Tokushima University / Educator and Researcher Directory --- Tomoyasu, Toshifumi

Personal Web Page

https://researchmap.jp/tomoyasutoshifumi (researchmap)

https://orcid.org/0009-0009-3724-3747 (ORCID)

Field of Study

○	Pathogenic Microbiology
○	Protein Engineering

Subject of Study

○	連鎖球菌の病原性発現機構 (Streptococcus, cytolysin, intermedilysin, cholesterol)
○	Study for function of molecular chaperons (molecular chaperone, heat shock)

Book / Paper

Book:

1.	Toshifumi Tomoyasu : 病原性微生物の取扱い, NTS Inc., Jul. 2014. (Keyword) 病原性微生物 / BSL / bacteria / 取り扱い
2.	小椋光, 龍田高志 and Toshifumi Tomoyasu : 細菌のストレス応答と分子シャペロン, シュプリンガーフェアラーク東京・共編:永田和宏，森正敬，吉田賢右, Jun. 2001. (Keyword) bacteria / FtsH / ストレス応答 / molecular chaperone

Academic Paper (Judged Full Paper):

1.	Takuya YAMADA, Yugo YAMAMORI, Nanami Matsuda, Hideaki Nagamune, Kazuto Ohkura, Toshifumi Tomoyasu and Atsushi Tabata : Streptolysin S induces pronounced calcium-ion influx-dependent expression of immediate early genes encoding transcription factors, Scientific Reports, Vol.13, No.13720, 2023. (Summary) Anginosus group streptococci (AGS) are opportunistic human pathogens of the oral cavity. The β-hemolytic subgroup of Streptococcus anginosus subsp. anginosus secretes streptolysin S (SLS) and exhibits not only hemolytic activity but also cytotoxicity toward cultured human cell lines. However, the detailed mechanism of action of SLS and the cellular responses of host cells have not yet been fully clarified. To determine the pathogenic potential of SLS-producing β-hemolytic S. anginosus subsp. anginosus, the SLS-dependent response induced in the human oral squamous cell carcinoma HSC-2 cells was investigated to determine the pathogenic potential of SLS-producing β-hemolytic S. anginosus subsp. anginosus. This study revealed that the Ca influx and the expression of immediate early genes (IEGs) encoding transcription factors such as early growth responses (EGRs) and activator protein-1 (AP-1) were greatly increased in HSC-2 cells incubated with the culture supernatant of SLS-producing β-hemolytic S. anginosus subsp. anginosus. Moreover, this SLS-dependent increase in expression was significantly suppressed by Ca chelation, except for jun. These results suggest that SLS caused Ca influx into the cells following greatly enhanced expression of IEG-encoding transcription factors. The results of this study may help in understanding the pathogenicity of SLS-producing AGS. (Keyword) cytolysin / Streptococcus (Link to Publication Site) ● Publication site (DOI): 10.1038/s41598-023-40981-1 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37608082 ● Search Scopus @ Elsevier (PMID): 37608082 ● Search Scopus @ Elsevier (DOI): 10.1038/s41598-023-40981-1 (DOI: 10.1038/s41598-023-40981-1, PubMed: 37608082)
2.	Toshifumi Tomoyasu, Airi Matsumoto, Ayuko Takao, Atsushi Tabata and Hideaki Nagamune : A simple method to differentiate three classes of cholesterol-dependent cytolysins., Journal of Microbiological Methods, Vol.207, 2023. (Summary) Cholesterol-dependent cytolysins (CDCs) are proteinaceous toxins widely distributed in gram-positive pathogenic bacteria. CDCs can be classified into three groups (I-III) based on the mode of receptor recognition. Group I CDCs recognize cholesterol as their receptor. Group II CDC specifically recognizes human CD59 as the primary receptor on the cell membrane. Only intermedilysin from Streptococcus intermedius has been reported as a group II CDC. Group III CDCs recognize both human CD59 and cholesterol as receptors. CD59 contains five disulfide bridges in its tertiary structure. Therefore, we treated human erythrocytes with dithiothreitol (DTT) to inactivate CD59 on membranes. Our data showed that DTT treatment caused a complete loss of recognition of intermedilysin and an anti-human CD59 monoclonal antibody. In contrast, this treatment did not affect the recognition of group I CDCs, judging from the fact that DTT-treated erythrocytes were lysed with the same efficiency as mock-treated human erythrocytes. The recognition of group III CDCs toward DTT-treated erythrocytes was partially reduced, and these results are likely due to the loss of human CD59 recognition. Therefore, the degree of human CD59 and cholesterol requirements of uncharacterized group III CDCs frequently found in Mitis group streptococci can be easily estimated by comparing the amounts of hemolysis between DTT-treated and mock-treated erythrocytes. (Keyword) bacterial toxins / Cytotoxins / Cell Membrane / Erythrocytes / cholesterol (Link to Publication Site) ● Publication site (DOI): 10.1016/j.mimet.2023.106696 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36898586 ● Search Scopus @ Elsevier (PMID): 36898586 ● Search Scopus @ Elsevier (DOI): 10.1016/j.mimet.2023.106696 (DOI: 10.1016/j.mimet.2023.106696, PubMed: 36898586)
3.	Shuto Yokohata, Kazuto Ohkura, Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Human serum albumin stabilizes streptolysin S activity secreted in the extracellular milieu by streptolysin S-producing streptococci., Microbiology and Immunology, Vol.67, No.2, 58-68, 2022. (Summary) Anginosus group streptococci (AGS) are opportunistic pathogens of the human oral cavity; however, their pathogenicity has not been discussed in detail. Oral streptococci live in the gingival sulcus, from where they can easily translocate into the bloodstream due to periodontal diseases and dental treatment and cause hazardous effects on the host through their virulence factors. Streptolysin S (SLS), a pathogenic factor produced by β-hemolytic species/strains belonging to AGS, plays an important role in damaging host cells. Therefore, we investigated the SLS-dependent cytotoxicity of β-hemolytic Streptococcus anginosus subsp. anginosus (SAA), focusing on different growth conditions such as in the bloodstream. Consequently, SLS-dependent hemolytic activity/cytotoxicity in the culture supernatant of β-hemolytic SAA was stabilized by blood components, particularly human serum albumin (HSA). The present study suggests that the secreted SLS, not only from β-hemolytic SAA, but also from other SLS-producing streptococci, is stabilized by HSA. As HSA is the most abundant protein in human plasma, the results of this study provide new insights into the risk of SLS-producing streptococci which can translocate into the bloodstream. (Keyword) Humans / Streptolysins / Serum Albumin, Human / Streptococcus pyogenes / Virulence / Virulence Factors / Bacterial Proteins (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.13042 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36478453 ● Search Scopus @ Elsevier (PMID): 36478453 ● Search Scopus @ Elsevier (DOI): 10.1111/1348-0421.13042 (DOI: 10.1111/1348-0421.13042, PubMed: 36478453)
4.	Atsushi Tabata, Airi Matsumoto, Ai Fujimoto, Kazuto Ohkura, Takuya Ikeda, Hiroki Oda, Shuto Yokohata, Miho Kobayashi, Toshifumi Tomoyasu, Ayuko Takao, Hisashi Ohkuni and Hideaki Nagamune : Dual functions of discoidinolysin, a cholesterol-dependent cytolysin with N-terminal discoidin domain produced from strain Nm-76., Journal of Oral Microbiology, Vol.14, No.1, 2105013, 2022. (Summary) Some strains of exhibit β-hemolysis due to the β-hemolytic activity of cholesterol-dependent cytolysin (CDC). Recently, a gene encoding an atypical lectinolysin-related CDC was found in strain Nm-76. However, the product of this gene remains uncharacterized. We aimed to characterize this atypical CDC and its molecular functions and contribution to the pathogenicity of strain Nm-76. Phylogenetic analysis of the CDC gene was conducted based on the web-deposited information. The molecular characteristics of CDC were investigated using a gene-deletion mutant strain and recombinant proteins expressed in . The gene encoding CDC found in Nm-76 and its homolog are distributed among many strains. This CDC is phylogenetically different from other previously characterized CDCs, such as -derived human platelet aggregation factor (Sm-hPAF)/lectinolysin and mitilysin. Because this CDC possesses an additional N-terminal domain, including a discoidin motif, it was termed discoidinolysin (DLY). In addition to the preferential lysis of human cells, DLY displayed N-terminal domain-dependent facilitation of human erythrocyte aggregation and intercellular associations between human cells. DLY functions as a hemolysin/cytolysin and erythrocyte aggregation/intercellular association molecule. This dual-function DLY could be an additional virulence factor in . (Link to Publication Site) ● Publication site (DOI): 10.1080/20002297.2022.2105013 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35937899 ● Search Scopus @ Elsevier (PMID): 35937899 ● Search Scopus @ Elsevier (DOI): 10.1080/20002297.2022.2105013 (DOI: 10.1080/20002297.2022.2105013, PubMed: 35937899)
5.	Atsushi Tabata, Rina Shirai, Haruka Miki, Yukihiro Nishikawa, Tatsuya Kashima, Tomomi Aoyama, Shu Murakami, Momoyo Azuma, Toshifumi Tomoyasu and Hideaki Nagamune : Hapten-labeled fusion-polymerase chain reaction of multiple marker genes for the application of immunochromatographic test., Journal of Bioscience and Bioengineering, Vol.134, No.1, 70-76, 2022. (Summary) A variety of methods have been reported using polymerase chain reaction (PCR)-based nucleic acid testing (NAT) because of its potential to be used in highly sensitive inspection systems. Among these NATs, fusion-PCR (also called as overlap-extension-PCR) has been focused on this study and adopted to generate the fused amplicon composed of plural marker gene fragments for detection. Generally, conventional agarose gel electrophoresis followed by gel staining is employed to check the PCR results. However, these are time-consuming processes that use specific equipment. To overcome these disadvantages, the immunochromatographic test (ICT) for the detection of PCR amplicons with hapten-labels that were generated by PCR using hapten-labeled primers was also adopted in this study. Based on these concepts, we constructed the systems of hapten-labeled fusion-PCR (HL-FuPCR) followed by ICT (HL-FuPCR-ICT) for the two and three marker genes derived from pathogenic microbe. As a result, we successfully developed a two marker genes system for the pathogenic influenza A virus and a three marker genes system for the penicillin-resistant Streptococcus pneumoniae. These detection systems of HL-FuPCR-ICT are characterized by simple handling and rapid detection within few minutes, and also showed the results as clear lines. Thus, the HL-FuPCR-ICT system introduced in this study has potential for use as a user-friendly inspection tool with the advantages especially in the detection of specific strains or groups expressing the characteristic phenotype(s) such as antibiotic resistance and/or high pathogenicity even in the same species. (Keyword) DNA Primers / Haptens / Immunologic Tests / Polymerase Chain Reaction / Sensitivity and Specificity (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jbiosc.2022.03.006 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35450786 ● Search Scopus @ Elsevier (PMID): 35450786 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jbiosc.2022.03.006 (DOI: 10.1016/j.jbiosc.2022.03.006, PubMed: 35450786)
6.	Airi Matsumoto, Atsushi Tabata, Kazuto Ohkura, Hiroki Oda, Chihiro Kodama, Hisashi Ohkuni, Ayuko Takao, Ken Kikuchi, Toshifumi Tomoyasu and Hideaki Nagamune : Molecular characteristics of an adhesion molecule containing cholesterol-dependent cytolysin-motif produced by mitis group streptococci, Microbiology and Immunology, Vol.65, No.2, 61-75, 2021. (Summary) Streptococcus pseudopneumoniae (SPpn) is a relatively new species closely related to S. pneumoniae (SPn) and S. mitis (SM) belonging to the Mitis group of the genus Streptococcus (MGS). Although genes encoding various pneumococcal virulence factors have been observed in the SPpn genome, the pathogenicity of SPpn against human, including the roles of virulence factor candidates, is still unclear. The present study focused on and characterized a candidate virulence factor previously reported in SPpn with deduced multiple functional domains, such as lipase domain, two lectin domains, and cholesterol-dependent cytolysin-related domain using various recombinant proteins. The gene was found not only in SPpn but also in the strains of SM and SPn. Moreover, the gene product was expressed in the gene-positive strains as secreted and cell-bound forms. The recombinant of gene product showed lipase activity and human cell-binding activity depending on the function of lectin domain(s), but no hemolytic activity. Thus, based on the distribution of the gene within the MGS and its molecular function, the gene product was named mitilectin (MLC) and its contribution to the potential pathogenicity of the MLC-producing strains was investigated. Consequently, the treatment with anti-MLC antibody and the mlc gene-knockout significantly reduced the human cell-binding activity of MLC-producing strains. Therefore, the multifunctional MLC was suggested to be important as an adhesion molecule in considering the potential pathogenicity of the MLC-producing strains belonging to MGS, such as SPpn and SM. (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.12868 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33331679 ● Search Scopus @ Elsevier (PMID): 33331679 ● Search Scopus @ Elsevier (DOI): 10.1111/1348-0421.12868 (DOI: 10.1111/1348-0421.12868, PubMed: 33331679)
7.	Atsushi Tabata, Hisashi Ohkuni, Yasuhiko Itoh, Yoshitaka Fukunaga, Toshifumi Tomoyasu and Hideaki Nagamune : Complete Genome Sequence of Streptococcus mitis Strain Nm-65, Isolated from a Patient with Kawasaki Disease, Microbiology Resource Announcements, Vol.10, No.1, e01239-20, 2021. (Summary) Nm-65 is a human commensal streptococcal strain of the mitis group that was isolated from the tooth surface of a patient with Kawasaki disease. The complete genome sequence of Nm-65 was obtained by means of hybrid assembly, using two next-generation sequencing data sets. The final assembly size was 2,085,837 bp, with 2,039 coding sequences. (Tokushima University Institutional Repository) ● Metadata: 116462 (Link to Publication Site) ● Publication site (DOI): 10.1128/MRA.01239-20 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33414340 ● Search Scopus @ Elsevier (PMID): 33414340 ● Search Scopus @ Elsevier (DOI): 10.1128/MRA.01239-20 (Tokushima University Institutional Repository: 116462, DOI: 10.1128/MRA.01239-20, PubMed: 33414340)
8.	Atsushi Tabata, Hisashi Ohkuni, Haruka Hino, Takuya Saigo, Chihiro Kodama, QING TANG, Toshifumi Tomoyasu, Yoshitaka Fukunaga, Yasuhiko Itoh and Hideaki Nagamune : Cytotoxic property of Streptococcus mitis strain producing two different types of cholesterol-dependent cytolysins, Infection, Genetics and Evolution, Vol.85, 104483, 2020. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.meegid.2020.104483 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32731044 ● Summary page in Scopus @ Elsevier: 2-s2.0-85088967403 (DOI: 10.1016/j.meegid.2020.104483, PubMed: 32731044, Elsevier: Scopus)
9.	Ayuko Takao, Toshifumi Tomoyasu, Atsushi Tabata, Hideaki Nagamune and Nobuko Maeda : A photometric pH assay for microplate bacterial cultures., Journal of Microbiological Methods, Vol.172, 1-3, 2020. (Summary) A photometric pH assay for sugar-fermenting bacterial culture on a 96-well plate was developed. This assay can save time and effort in repeat handlings. Its use could decrease the risk of bacterial contamination in measurement devices and leakage into the environment. The assay's pH estimation range was pH 4.2-7.6. (Keyword) chemical indicators / fermentation / pH assay / photometric method / microbial culture (Link to Publication Site) ● Publication site (DOI): 10.1016/j.mimet.2020.105910 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32229266 ● Summary page in Scopus @ Elsevier: 2-s2.0-85082519032 (DOI: 10.1016/j.mimet.2020.105910, PubMed: 32229266, Elsevier: Scopus)
10.	Atsushi Tabata, Takuya Yamada, Ohtani Hiromi, Kazuto Ohkura, Toshifumi Tomoyasu and Hideaki Nagamune : β-Hemolytic Streptococcus anginosus subsp. anginosus causes streptolysin S-dependent cytotoxicity to human cell culture lines in vitro, Journal of Oral Microbiology, Vol.11, No.1, 1-11, 2019. (Summary) Streptococcus anginosus subsp. (SAA) is one of the opportunistic pathogens in humans that inhabits the oral cavity. The type strain of SAA, NCTC10713, showed clear β-hemolysis on blood agar plates, and the sole β-hemolytic factor revealed two streptolysin S (SLS) molecules. SLS is well known as the peptide hemolysin produced from the human pathogen and shows not only hemolytic activity on erythrocytes but also cytotoxic activity in cell culture lines and , such as in a mouse infection model. However, no cytotoxic activity of SLS produced from β-hemolytic SAA (β-SAA) has been reported so far. In this study, the SLS-dependent cytotoxicity of the β-SAA strains including the genetically modified strains was investigated . The SLS-producing β-SAA showed cytotoxicity in human cell culture lines under the co-cultivation condition and it was found that this cytotoxicity was caused by the SLS secreted into the extracellular milieu. The results from this study suggest that the SLS produced from β-SAA might indicate the cytotoxic potential similar to that of the SLS from and the SLS-producing β-SAA would be recognized as "a wolf in sheep's clothing" More attention will be paid to the pathogenicity of β-hemolytic Anginosus group streptococci. (Keyword) bacterial toxins / Streptococcus (Tokushima University Institutional Repository) ● Metadata: 113540 (Link to Publication Site) ● Publication site (DOI): 10.1080/20002297.2019.1609839 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31105901 ● Summary page in Scopus @ Elsevier: 2-s2.0-85065585236 (Tokushima University Institutional Repository: 113540, DOI: 10.1080/20002297.2019.1609839, PubMed: 31105901, Elsevier: Scopus)
11.	Toshifumi Tomoyasu, Keigo Tsuruno, Ryosuke Tanatsugu, Aya Miyazaki, Hiroyuki Kondo, Atsushi Tabata, Whiley A. Robert, Kenji Sonomoto and Hideaki Nagamune : Recognizability of heterologous co-chaperones with Streptococcus intermedius DnaK and Escherichia coli DnaK, Microbiology and Immunology, Vol.62, No.11, 681-693, 2018. (Summary) Streptococcus intermedius DnaK complements the temperature-sensitive phenotype of an Escherichia coli dnaK null mutant only when co-chaperones DnaJ and GrpE are co-expressed. Therefore, whether S. intermedius DnaK and E. coli DnaK can recognize heterologous co-chaperones in vitro was examined. Addition of heterologous GrpE to DnaK and DnaJ partially stimulated adenosine triphosphatase (ATPase) activity, and almost completely stimulated luciferase refolding activity. Addition of heterologous DnaJ to GrpE and DnaK also stimulated ATPase activity; however, significant luciferase refolding activity was not observed. Moreover, E. coli DnaJ had a negative effect on the luciferase refolding activity of the S. intermedius DnaK chaperone system. In E. coli chaperone mutants, with the exception of E. coli DnaJ, stronger expression of the heterologous co-chaperones partially or almost completely complemented the temperature-sensitive-phenotype. These results indicate that all heterologous co-chaperones can at least partially recognize DnaK of a distantly related species. A region of the ATPase domain that is present in the DnaK of gram-negative bacteria is absent from the DnaK of gram-positive bacteria. This region is believed to be important for recognition of co-chaperones from gram-negative bacteria. However, insertion of this segment into S. intermedius DnaK failed to increase its ability to recognize E. coli co-chaperones, implying that this region is unnecessary or insufficient for the recognition of E. coli co-chaperones. Thus, our data suggest that a basic structural similarity is conserved among the components of the S. intermedius and E. coli DnaK chaperone systems, allowing weak associations between heterologous components. (Keyword) molecular chaperone / Escherichia coli / Streptococcus (Tokushima University Institutional Repository) ● Metadata: 115748 (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.12651 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30239035 ● Summary page in Scopus @ Elsevier: 2-s2.0-85056121796 (Tokushima University Institutional Repository: 115748, DOI: 10.1111/1348-0421.12651, PubMed: 30239035, Elsevier: Scopus)
12.	Qing Tang, Masayoshi Onitsuka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Construction of Anti-HER2 Recombinants as Targeting Modules for a Drug-delivery System Against HER2-positive Cells, Anticancer Research, Vol.38, No.7, 4319-4325, 2018. (Summary) Recombinant antibodies have been investigated and used in applications such as targeting modules of drug-delivery systems (DDS) against cancers. This study aimed to prepare recombinant antibodies against HER2, containing sortase A (SrtA) recognition sequence, that are applicable as targeting modules in DDS after linkage with the drug-carrier containing oligoglycine-acceptor peptide by SrtA transpeptidation. The recombinant trastuzumab fragment antibodies (scFvs and Fab) with the SrtA-recognition motif (LPXTG) at their C-terminal were constructed and expressed in Escherichia coli and Chinese hamster ovary (CHO) cells, respectively. The reactivity of the purified recombinant antibodies towards HER2-expressing cells was also evaluated via immunofluorescent staining. Fab demonstrated higher yield and purity and better reactivity towards HER2-expressing cells (HCT-15 and HeLa) when compared to scFvs. The CHO expression system possesses superior yield and purity when compared to the E. coli expression system with respect to the preparation of recombinant antibodies applicable in targeting modules for DDS (DDS-TM). Moreover, a Fab variant prepared in this study demonstrated the potential to be a DDS-TM against HER2-expressing cancer cells. (Keyword) drug delivery system / cancer therapy (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.12731 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29970568 ● Summary page in Scopus @ Elsevier: 2-s2.0-85049804969 (DOI: 10.21873/anticanres.12731, PubMed: 29970568, Elsevier: Scopus)
13.	Toshifumi Tomoyasu, Masaki Matoba, Ayuko Takao, Atsushi Tabata, A Robert. Whiley, Nobuko Maeda and Hideaki Nagamune : Rapid screening method for detecting highly pathogenic Streptococcus intermedius strains carrying a mutation in the lacR gene., FEMS Microbiology Letters, Vol.365, No.3, fnx-258, 2018. (Summary) Streptococcus intermedius is a member of the normal human commensal flora and secretes a human-specific cytolysin intermedilysin (ILY) as a major virulence factor. Expression of ily is repressed by LacR and loss-of-function mutations of LacR are observed in many ILY high-producing strains isolated from deep-seated abscesses, suggesting that high ILY production is necessary for increased virulence. However, because ILY exhibits no β-hemolysis on animal blood agar plates, differentiating ILY high- and low-producing strains using conventional laboratory methods is not possible. Interestingly, S. intermedius also produces glycosidases, including MsgA and NanA, which exhibit N-acetyl-β-d-glucosaminidase and neuraminidase activities, respectively. Moreover, MsgA expression, but not NanA, is negatively regulated by LacR. Here we measured the activities of MsgA, NanA and ILY in strains isolated from clinical specimens and dental plaque to determine the correlation between these glycosidase activities and ILY hemolytic activity. Hemolytic activity showed a strong positive correlation with MsgA and a weak negative correlation with NanA activities. Therefore, we calculated the ratio of MsgA and NanA activity (M/N ratio). This value showed a stronger positive correlation (r = 0.81) with ILY hemolytic activity and many strains with high M/N ratios (>2) were ILY-high producers with loss-of-function mutations in LacR. (Keyword) pathogenic microorganism / virulence factor (Tokushima University Institutional Repository) ● Metadata: 115749 (Link to Publication Site) ● Publication site (DOI): 10.1093/femsle/fnx258 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29228148 ● Summary page in Scopus @ Elsevier: 2-s2.0-85056596012 (Tokushima University Institutional Repository: 115749, DOI: 10.1093/femsle/fnx258, PubMed: 29228148, Elsevier: Scopus)
14.	Atsushi Tabata, Douglas Deutsch, Seiya Otsuka, Kathleen Verratti, Toshifumi Tomoyasu, Hideaki Nagamune and A. Vincent Fischetti : A novel plasmid, pSAA0430-08, from Streptococcus anginosus subsp. anginosus strain 0430-08, Plasmid, Vol.95, No.1, 16-27, 2018. (Summary) Mobile genetic elements (MGEs) are the genetic material often involved in the interspecies and intraspecies genetic transduction in bacteria. However, little is known about MGEs in the Anginosus group of streptococci (AGS), one of the streptococcal groups found in the oral cavity of humans. We looked for the presence of MGEs in Streptococcus anginosus subsp. anginosus (SAA), a representative species belonging to AGS, and found a novel plasmid from SAA strain 0430-08. This plasmid was 7038bp and ~31% G/C content which we named pSAA0430-08, and examined its genetic structure and characteristics. Open reading frame (ORF) prediction revealed that pSAA0430-08 was composed of 10 ORFs including a putative plasmid replication protein (ORF1) and a putative toxin-antitoxin system (ORF9 and ORF10). Between ORF10 and ORF 1, four tandem repeats of 22bp each, generally termed as iteron, were also observed. Using variant plasmids of pSAA0430-08, we confirmed that both ORF1 and iteron were necessary for replication in host cells. Interestingly, the region from ORF4 to ORF7 showed homology with a genomic DNA segment of S. gordonii strains. Thus, this plasmid may travel between the different species in Streptococci, i.e., S. gordonii and S. anginosus. (Keyword) pathogenic microorganism / Plasmid (Link to Publication Site) ● Publication site (DOI): 10.1016/j.plasmid.2018.01.002 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29355570 ● Summary page in Scopus @ Elsevier: 2-s2.0-85041495681 (DOI: 10.1016/j.plasmid.2018.01.002, PubMed: 29355570, Elsevier: Scopus)
15.	Toshifumi Tomoyasu, Takahiro Yamasaki, Shinya Chiba, Shingo Kusaka, Atsushi Tabata, Robert A. Whiley and Hideaki Nagamune : Positive- and Negative-Control Pathways by Blood Components for Intermedilysin Production in Streptococcus intermedius., Infection and Immunity, Vol.85, No.9, 1-17, 2017. (Summary) is an opportunistic bacterial pathogen secreting a human-specific cytolysin called intermedilysin (ILY) as a major pathogenic factor. This bacterium can degrade glycans into monosaccharides using two glycosidases, multisubstrate glycosidase A (MsgA) and neuraminidase (NanA). Here, we detected a stronger hemolytic activity mediated by ILY when PC574 was cultured in fetal bovine serum (FBS) than when it was grown in the standard culture medium. FBS-cultured cells also showed higher MsgA and NanA activity, although overproduction of ILY in FBS was undetectable in mutants -null and -null. Addition of purified MsgA and NanA to the FBS resulted in a release of 2.8 mM galactose and 4.3 mM -acetylneuraminic acid; these sugar concentrations were sufficient to upregulate the expression of ILY, MsgA, and NanA. Conversely, when strain PC574 was cultured in human plasma, no similar increase in hemolytic activity was observed. Moreover, addition of human plasma to the culture in FBS appeared to inhibit the stimulatory effect of FBS on ILY, MsgA, and NanA, although there were individual differences among the plasma samples. We confirmed that human plasma contains immunoglobulins that can neutralize ILY, MsgA, and NanA activities. In addition, human plasma had a neutralizing effect on cytotoxicity of toward HepG2 cells in FBS, and a higher concentration of human plasma was necessary to reduce the cytotoxicity of an ILY-high-producing strain than an ILY-low-producing strain. Overall, our data show that blood contains factors that stimulate and inhibit ILY expression and activity, which may affect pathogenicity of . (Keyword) Streptococcus intermedius / intermedilysin / cytolysin / sugar chain / antibody (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.00379-17 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28607101 ● Summary page in Scopus @ Elsevier: 2-s2.0-85027524694 (DOI: 10.1128/IAI.00379-17, PubMed: 28607101, Elsevier: Scopus)
16.	Atsushi Tabata, Ohkubo Yukihisa, Natsuki Anyhoji, Keiko Hojo, Toshifumi Tomoyasu, Youhei Tatematsu, Kazuto Ohkura and Hideaki Nagamune : Development of a Sortase A-mediated Peptide-labeled Liposome Applicable to Drug-delivery Systems, Anticancer Research, Vol.35, No.8, 4411-4417, 2015. (Summary) In order to develop an efficient drug-delivery system (DDS), a lipopeptide-loaded liposome that functions as a platform for the transpeptidase reaction mediated by sortase A (SrtA) was constructed and its stability, as well as cell-specific targeting were evaluated in the present study. Several lipopeptides possessing an acceptor peptide sequence (oligoglycine ≥ three residues) or donor peptide sequence (LPETG) for the SrtA-mediated reaction were chemically synthesized and then inserted into the liposome membrane composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and cholesterol (DPPC-Chol-lipo) to obtain the lipopeptide-loaded liposomes. The transpeptidase reaction mediated by recombinant SrtA (His-ΔN59SrtA) was employed to modify the peptide moiety on the liposomal surface using a fluorescently-labeled substrate peptide corresponding to the species of each loaded lipopeptide. Furthermore, lung tumor-binding peptide (LTBP)-labeled liposomes, prepared by this transpeptidase reaction, were investigated for selective targeting to lung cancer cells in vitro. The His-ΔN59SrtA-mediated transpeptidation of fluorescently-labeled peptide on the lipopeptide-loaded DPPC-Chol-lipo was confirmed. The selective targeting of LTBP-labeled liposomes to the lung cancer cell line A549 was also observed in vitro. These results suggest that the labeling of acceptor or donor lipopeptide-loaded liposomes with the transpeptidase SrtA could be a useful method for developing a platform applicable to a cancer-targeting DDS. (Keyword) drug delivery system / liposomes (Tokushima University Institutional Repository) ● Metadata: 117781 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26168480 ● Summary page in Scopus @ Elsevier: 2-s2.0-84939824857 (Tokushima University Institutional Repository: 117781, PubMed: 26168480, Elsevier: Scopus)
17.	Kim Hyejin, Atsushi Tabata, Toshifumi Tomoyasu, Ueno Tomomi, Uchiyama Shigeto, Keizo Yuasa, Akihiko Tsuji and Hideaki Nagamune : Estrogen stimuli promote osteoblastic differentiation via the subtilisin-like proprotein convertase PACE4 in MC3T3-E1 cells., Journal of Bone and Mineral Metabolism, Vol.33, No.1, 30-39, 2015. (Summary) Estrogenic compounds include endogenous estrogens such as estradiol as well as soybean isoflavones, such as daidzein and its metabolite equol, which are known phytoestrogens that prevent osteoporosis in postmenopausal women. Indeed, mineralization of MC3T3-E1 cells, a murine osteoblastic cell line, was significantly decreased in medium containing fetal bovine serum treated with charcoal-dextran to deplete endogenous estrogens, but estradiol and these soybean isoflavones dose-dependently restored the differentiation of MC3T3-E1 cells; equal was tenfold more effective than daidzein. These differentiation promoting effects were inhibited by the addition of fulvestrant, which is a selective downregulator of estrogen receptors. Analysis of the expression pattern of bone-related genes by reverse transcription PCR (RT-PCR)/quantitative real-time PCR (qRT-PCR), which focused on responsiveness to the estrogen stimuli, revealed that the transcription of PACE4, a subtilisin-like proprotein convertase, was tightly linked with the differentiation of MC3T3-E1 cells induced by estrogen stimuli. Moreover, treatment with RNAi of PACE4 in MC3T3-E1 cells resulted in a drastic decrease of mineralization in the presence of estrogen stimuli. These results strongly suggest that PACE4 participates in bone formation at least in osteoblast differentiation, and estrogen receptor-mediated stimuli induce osteoblast differentiation through the upregulation of PACE4 expression. (Keyword) osteoblast / PACE4 / Estrogen / Soybean / isoflavone (Link to Publication Site) ● Publication site (DOI): 10.1007/s00774-014-0567-9 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24557631 ● Summary page in Scopus @ Elsevier: 2-s2.0-84893948353 (DOI: 10.1007/s00774-014-0567-9, PubMed: 24557631, Elsevier: Scopus)
18.	Atsushi Tabata, Natsuki Anyoji, Yukimasa Ohkubo, Toshifumi Tomoyasu and Hideaki Nagamune : Investigation on the Reaction Conditions of Staphylococcus aureus Sortase A for Creating Surface-modified Liposomes as a Drug-delivery System Tool, Anticancer Research, Vol.34, No.8, 4521-4527, 2014. (Summary) This study aimed to determine the preferred conditions for the transpeptidase reaction of sortase A from Staphylococcus aureus, for the purpose of creating functional liposomes useful for a drug-delivery system (DDS). His-tagged recombinant sortase A with 59 amino acids deleted from the N-terminus (His-ΔN59SrtA) was prepared using an Escherichia coli expression system. The pH dependency and sorting signal sequence dependency of the transpeptidase reaction of His-ΔN59SrtA were analyzed by monitoring the transfer of model donor-substrates (i.e. His-tagged mutant green fluorescent proteins with a C-terminal LPxTG sorting signal) to model acceptor-beads with a GGGGGC peptide. In addition, using preferred conditions, the sortase A reaction was used to modify liposome surface. The transpeptidase reaction of His-ΔN59SrtA was enhanced under weakly acidic conditions. Transfer efficiency, based on sorting signal recognition by His-ΔN59SrtA, was similar to or higher than that obtained using several substrates with amino acids other than Glu in the sorting signal position "x". Furthermore, liposomes containing GGGGGC peptide-linked dipalmitoylphosphatidylethanolamine were successfully modified using the preferred conditions for His-ΔN59SrtA determined in this study. Preferred conditions for the transpeptidase reaction of His-ΔN59SrtA, especially in a weakly acidic environment to enhance reaction, was established and successfully used to create functional liposomes applicable to DDS. (Keyword) Sortase A (Tokushima University Institutional Repository) ● Metadata: 117782 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25075095 ● Summary page in Scopus @ Elsevier: 2-s2.0-84908660909 (Tokushima University Institutional Repository: 117782, PubMed: 25075095, Elsevier: Scopus)
19.	Hidenori Imaki, Toshifumi Tomoyasu, Naoki Yamamoto, Chiharu Taue, Sachiko Masuda, Ayuko Takao, Nobuko Maeda, Atsushi Tabata, Robert A. Whiley and Hideaki Nagamune : Identification and Characterization of a Novel Secreted Glycosidase with Multiple Glycosidase Activities in Streptococcus intermedius, Journal of Bacteriology, Vol.196, No.15, 2817-2826, 2014. (Summary) Streptococcus intermedius is a known human pathogen and belongs to the anginosus group (S. anginosus, S. intermedius, and S. constellatus) of streptococci (AGS). We found a large open reading frame (6,708 bp) in the lac operon, and bioinformatic analysis suggested that this gene encodes a novel glycosidase that can exhibit β-d-galactosidase and N-acetyl-β-d-hexosaminidase activities. We, therefore, named this protein "multisubstrate glycosidase A" (MsgA). To test whether MsgA has these glycosidase activities, the msgA gene was disrupted in S. intermedius. The msgA-deficient mutant no longer showed cell- and supernatant-associated β-d-galactosidase, β-d-fucosidase, N-acetyl-β-d-glucosaminidase, and N-acetyl-β-d-galactosaminidase activities, and all phenotypes were complemented in trans with a recombinant plasmid carrying msgA. Purified MsgA had all four of these glycosidase activities and exhibited the lowest Km with 4-methylumbelliferyl-linked N-acetyl-β-d-glucosaminide and the highest kcat with 4-methylumbelliferyl-linked β-d-galactopyranoside. In addition, the purified LacZ domain of MsgA had β-d-galactosidase and β-d-fucosidase activities, and the GH20 domain exhibited both N-acetyl-β-d-glucosaminidase and N-acetyl-β-d-galactosaminidase activities. The β-d-galactosidase and β-d-fucosidase activities of MsgA are thermolabile, and the optimal temperature of the reaction was 40°C, whereas almost all enzymatic activities disappeared at 49°C. The optimal temperatures for the N-acetyl-β-d-glucosaminidase and N-acetyl-β-d-galactosaminidase activities were 58 and 55°C, respectively. The requirement of sialidase treatment to remove sialic acid residues of the glycan branch end for glycan degradation by MsgA on human α1-antitrypsin indicates that MsgA has exoglycosidase activities. MsgA and sialidase might have an important function in the production and utilization of monosaccharides from oligosaccharides, such as glycans for survival in a normal habitat and for pathogenicity of S. intermedius. (Keyword) Streptococcus intermedius / glycosidase / multi-substrates glycosidase (Link to Publication Site) ● Publication site (DOI): 10.1128/JB.01727-14 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24858187 ● Summary page in Scopus @ Elsevier: 2-s2.0-84903904703 (DOI: 10.1128/JB.01727-14, PubMed: 24858187, Elsevier: Scopus)
20.	Atsushi Tabata, Yuji Sato, Kentaro Maya, Kota Nakano, Ken Kikuchi, Robert A. Whiley, Kazuto Ohkura, Toshifumi Tomoyasu and Hideaki Nagamune : A streptolysin S homologue is essential for beta-haemolytic Streptococcus constellatus subsp. constellatus cytotoxicit, Microbiology, Vol.160, No.5, 980-991, 2014. (Summary) Streptococcus constellatus is a member of the Anginosus group streptococci (AGS) and primarily inhabits the human oral cavity. S. constellatus is composed of three subspecies: S. constellatus subsp. constellatus (SCC), S. constellatus subsp. pharyngis and the newly described subspecies S. constellatus subsp. viborgensis. Although previous studies have established that SCC contains β-haemolytic strains, the factor(s) responsible for β-haemolysis in β-haemolytic SCC (β-SCC) has yet to be clarified. Recently, we discovered that a streptolysin S (SLS) homologue is the β-haemolytic factor of β-haemolytic Streptococcus anginosus subsp. anginosus (β-SAA), another member of the AGS. Furthermore, because previous studies have suggested that other AGS species, except for Streptococcus intermedius, do not possess a haemolysin(s) belonging to the family of cholesterol-dependent cytolysins, we hypothesized that, as with β-SAA, the SLS homologue is the β-haemolytic factor of β-SCC, and therefore aimed to investigate and characterize the haemolytic factor of β-SCC in the present study. PCR amplification revealed that all of the tested β-SCC strains were positive for the sagA homologue of SCC (sagA(SCC)). Further investigations using β-SCC strain W277 were conducted to elucidate the relationship between sagA(SCC) and β-haemolysis by constructing sagA(SCC) deletion mutants, which completely lost β-haemolytic activity. This loss of β-haemolytic activity was restored by trans-complementation of sagA(SCC). Furthermore, a co-cultivation assay established that the cytotoxicity of β-SCC was clearly dependent on the presence of sagA(SCC). These results demonstrate that sagA(SCC) is the factor responsible for β-SCC β-haemolysis and cytotoxicity. (Keyword) Streptolysin S / Streptococcus constellatus / beta-hemolytic / cytotoxicity (Link to Publication Site) ● Publication site (DOI): 10.1099/mic.0.075580-0 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24600025 ● Search Scopus @ Elsevier (PMID): 24600025 ● Search Scopus @ Elsevier (DOI): 10.1099/mic.0.075580-0 (DOI: 10.1099/mic.0.075580-0, PubMed: 24600025)
21.	Atsushi Tabata, Kazuto Ohkura, Ohkubo Yukimasa, Toshifumi Tomoyasu, Ohkuni Hisashi, Whiley A. Robert and Hideaki Nagamune : The diversity of receptor recognition in cholesterol-dependent cytolysins, Microbiology and Immunology, Vol.58, No.3, 155-171, 2014. (Summary) Cholesterol-dependent cytolysins (CDCs) are bacterial pore-forming toxins secreted mainly by pathogenic Gram-positive bacteria. CDCs generally recognize and bind to membrane cholesterol to create pores and lyse target cells. However, in contrast to typical CDCs such as streptolysin O, several atypical CDCs have been reported. The first of these was intermedilysin, which is secreted by Streptococcus intermedius and has human cell-specificity, human CD59 (huCD59) being its receptor. In the study reported here, the diversity of receptor recognition among CDCs was investigated and multi-receptor recognition characteristics were identified within this toxin family. Streptococcus mitis-derived human platelet aggregation factor (Sm-hPAF) secreted by S. mitis strain Nm-65 isolated from a patient with Kawasaki disease was previously shown to hemolyze erythrocytes in a species-dependent manner, its maximum activity being in human cells. In the present study, it was found that Sm-hPAF recognizes both membrane cholesterol and huCD59 as receptors for triggering pore-formation. Moreover, vaginolysin (VLY) of Gardnerella vaginalis showed similar characteristics to Sm-hPAF regarding receptor recognition. On the basis of the results presented here, the mode of receptor recognition of CDCs can be categorized into the following three groups: (i) Group I, comprising typical CDCs with high affinity to cholesterol and no or very little affinity to huCD59; (ii) Group II, including atypical CDCs such as ILY, with no or very little affinity to cholesterol and high affinity to huCD59; and (iii) Group III, which contains atypical CDCs such as Sm-hPAF and VLY with affinity to both cholesterol and huCD59. (Keyword) cytolysin / cholesterol-dependet cytolysin / diversity (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.12131 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24401114 ● CiNii @ National Institute of Informatics (CRID): 1520291853530158464 ● Summary page in Scopus @ Elsevier: 2-s2.0-84895562361 (DOI: 10.1111/1348-0421.12131, PubMed: 24401114, CiNii: 1520291853530158464, Elsevier: Scopus)
22.	Toshifumi Tomoyasu, Hidenori Imaki, Sachiko Masuda, Ayumi Okamoto, HyeJin Kim, Richard Waite, Robert Whiley, Ken Kikuchi, Keiichi Hiramatsu, Atsushi Tabata and Hideaki Nagamune : LacR mutations are frequently observed in Streptococcus intermedius and are responsible for increased intermedilysin production and virulence., Infection and Immunity, Vol.81, No.9, 3276-3286, 2013. (Summary) Streptococcus intermedius secretes a human-specific cytolysin, intermedilysin (ILY), which is considered to be the major virulence factor of this pathogen. We screened for a repressor of ily expression by using random gene disruption in a low-ILY-producing strain (PC574). Three independent high-ILY-producing colonies that had plasmid insertions within a gene that has high homology to lacR were isolated. Validation of these observations was achieved through disruption of lacR in strain PC574 with an erythromycin cassette, which also led to higher hemolytic activity, increased transcription of ily, and higher cytotoxicity against HepG2 cells, compared to the parental strain. The direct binding of LacR within the ily promoter region was shown by a biotinylated DNA probe pulldown assay, and the amount of ILY secreted into the culture supernatant by PC574 cells was increased by adding lactose or galactose to the medium as a carbon source. Furthermore, we examined lacR nucleotide sequences and the hemolytic activity of 50 strains isolated from clinical infections and 7 strains isolated from dental plaque. Of the 50 strains isolated from infections, 13 showed high ILY production, 11 of these 13 strains had one or more point mutations and/or an insertion mutation in LacR, and almost all mutations were associated with a marked decline in LacR function. These results strongly suggest that mutation in lacR is required for the overproduction of ILY, which is associated with an increase in pathogenicity of S. intermedius. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / gene expression (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.00638-13 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23798532 ● Summary page in Scopus @ Elsevier: 2-s2.0-84884217618 (DOI: 10.1128/IAI.00638-13, PubMed: 23798532, Elsevier: Scopus)
23.	Atsushi Tabata, Yukimasa Ohkubo, Masato Tamura, Toshifumi Tomoyasu, Kazuto Ohkura and Hideaki Nagamune : Construction of an improved drug delivery system tool with enhanced versatility in cell-targeting., Anticancer Research, Vol.33, No.7, 2905-2910, 2013. (Summary) His-Z-CDC(ss)(IS) was revealed to be an improved DDS tool with enhanced versatility in cell targeting. (Keyword) Carcinoembryonic Antigen / Cell Membrane / Cells, Cultured / cholesterol / Drug Delivery Systems / Fibroblasts / Fluorouracil / Hemolysis / Hep G2 Cells / Humans / Immunoglobulin G / liposomes / Perforin / Protein Transport / Recombinant Fusion Proteins / Staphylococcus aureus (Tokushima University Institutional Repository) ● Metadata: 117783 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23780978 ● Search Scopus @ Elsevier (PMID): 23780978 (Tokushima University Institutional Repository: 117783, PubMed: 23780978)
24.	Atsushi Tabata, Kota Nakano, Kazuto Ohkura, Toshifumi Tomoyasu, Ken Kikuchi, Robert Whiley and Hideaki Nagamune : Novel Twin Streptolysin S-Like Peptides Encoded in the sag Operon Homologue of Beta-Hemolytic Streptococcus anginosus., Journal of Bacteriology, Vol.195, No.5, 1090-1099, 2013. (Summary) Streptococcus anginosus is a member of the anginosus group streptococci, which form part of the normal human oral flora. In contrast to the pyogenic group streptococci, our knowledge of the virulence factors of the anginosus group streptococci, including S. anginosus, is not sufficient to allow a clear understanding of the basis of their pathogenicity. Generally, hemolysins are thought to be important virulence factors in streptococcal infections. In the present study, a sag operon homologue was shown to be responsible for beta-hemolysis in S. anginosus strains by random gene knockout. Interestingly, contrary to pyogenic group streptococci, beta-hemolytic S. anginosus was shown to have two tandem sagA homologues, encoding streptolysin S (SLS)-like peptides, in the sag operon homologue. Gene deletion and complementation experiments revealed that both genes were functional, and these SLS-like peptides were essential for beta-hemolysis in beta-hemolytic S. anginosus. Furthermore, the amino acid sequence of these SLS-like peptides differed from that of the typical SLS of S. pyogenes, especially in their propeptide domain, and an amino acid residue indicated to be important for the cytolytic activity of SLS in S. pyogenes was deleted in both S. anginosus homologues. These data suggest that SLS-like peptides encoded by two sagA homologues in beta-hemolytic S. anginosus may be potential virulence factors with a different structure essential for hemolytic activity and/or the maturation process compared to the typical SLS present in pyogenic group streptococci. (Keyword) Streptococcus / Streptolysin S (Tokushima University Institutional Repository) ● Metadata: 117785 (Link to Publication Site) ● Publication site (DOI): 10.1128/JB.01344-12 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23292771 ● Search Scopus @ Elsevier (PMID): 23292771 ● Search Scopus @ Elsevier (DOI): 10.1128/JB.01344-12 (Tokushima University Institutional Repository: 117785, DOI: 10.1128/JB.01344-12, PubMed: 23292771)
25.	Toshifumi Tomoyasu, Atsushi Tabata, Yoko Ishikawa, Robert Whiley and Hideaki Nagamune : Small heat shock protein AgsA: an effective stabilizer of enzyme activities., Journal of Bioscience and Bioengineering, Vol.115, No.1, 15-19, 2013. (Summary) A small heat shock protein, AgsA, possesses chaperone activity that can reduce the amount of heat-aggregated protein in vivo, and suppress the aggregation of chemical- and heat-denatured proteins in vitro. Therefore, we examined the ability of AgsA to stabilize the activity of several enzymes by using this chaperone activity. We observed that AgsA can stabilize the enzymatic activities of Renilla (Renilla reniformis) luciferase, firefly (Photinus pyralis) luciferase, and β-galactosidase, and showed comparable or greater stabilization of these enzymes than bovine serum albumin (BSA), a well-known stabilizer of enzyme activities. In particular, AgsA revealed better stabilization of Renilla luciferase and β-galactosidase than BSA under disulfide bond-reducing conditions with dithiothreitol. In addition, AgsA also increased the enzymatic performance of β-galactosidase and various restriction enzymes to a comparable or greater extent than BSA. These data indicate that AgsA may be useful as a general stabilizer of enzyme activities. (Keyword) Small heat shock protein / HSP / enzyme (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jbiosc.2012.08.001 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22929984 ● Search Scopus @ Elsevier (PMID): 22929984 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jbiosc.2012.08.001 (DOI: 10.1016/j.jbiosc.2012.08.001, PubMed: 22929984)
26.	Atsushi Tabata, Yukimasa Ohkubo, Eriko Sakakura, Toshifumi Tomoyasu, Kazuto Ohkura and Hideaki Nagamune : Investigation of a Bacterial Pore-forming Chimera Toxin for Application as a Novel Drug-delivery System Tool, Anticancer Research, Vol.32, No.6, 2323-2330, 2012. (Summary) Cholesterol-dependent cytolysins (CDCs) are pore-forming toxins from Gram-positive bacteria. The aim of this study was to investigate the potential of a CDC, intermedilysin, as a drug-delivery system (DDS) for clinical application. Intermedilysin was modified by the addition of a disulfide bridge to regulate pore formation, by swapping domain 4 to provide cholesterol-binding capacity, and by the introduction of a targeting domain. The resultant chimera protein, His-LTBP-CDC(ss)(IP), was investigated for its use as a DDS tool in vitro. His-LTBP-CDC(ss)(IP) exhibited a regulated pore-forming capacity under reducing conditions. This chimera protein was able to deliver a drug-carrier liposome specifically to the target cell, to be endocytosed into the cell with subsequent release of the components into the cytoplasm. A chimera protein derived from the bacterial pore-forming toxin intermedilysin (His-LTBP-CDC(ss)(IP)) forms the basis for a novel DDS tool. (Keyword) Bacteriocins / Cell Line, Tumor / Drug Delivery Systems / Electrophoresis, Polyacrylamide Gel / Humans / Liposomes / Microscopy, Fluorescence / Recombinant Fusion Proteins (Tokushima University Institutional Repository) ● Metadata: 117784 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22641669 ● Summary page in Scopus @ Elsevier: 2-s2.0-84864557140 (Tokushima University Institutional Repository: 117784, PubMed: 22641669, Elsevier: Scopus)
27.	Toshifumi Tomoyasu, Atsushi Tabata, Hidenori Imaki, Keigo Tsuruno, Aya Miyazaki, Kenji Sonomoto, Robert Whiley and Hideaki Nagamune : Role of Streptococcus intermedius DnaK chaperone system in stress tolerance and pathogenicity, Cell Stress & Chaperones, Vol.17, No.1, 41-55, 2012. (Summary) Streptococcus intermedius is a facultatively anaerobic, opportunistic pathogen that causes purulent infections and abscess formation. The DnaK chaperone system has been characterized in several pathogenic bacteria and seems to have important functions in stress resistance and pathogenicity. However, the role of DnaK in S. intermedius remains unclear. Therefore, we constructed a dnaK knockout mutant that exhibited slow growth, thermosensitivity, accumulation of GroEL in the cell, and reduced cytotoxicity to HepG2 cells. The level of secretion of a major pathogenic factor, intermedilysin, was not affected by dnaK mutation. We further examined the function and property of the S. intermedius DnaK chaperone system by using Escherichia coli ΔdnaK and ΔrpoH mutant strains. S. intermedius DnaK could not complement the thermosensitivity of E. coli ΔdnaK mutant. However, the intact S. intermedius DnaK chaperone system could complement the thermosensitivity and acid sensitivity of E. coli ΔdnaK mutant. The S. intermedius DnaK chaperone system could regulate the activity and stability of the heat shock transcription factor ς(32) in E. coli, although S. intermedius does not utilize ς(32) for heat shock transcription. The S. intermedius DnaK chaperone system was also able to efficiently eliminate the aggregated proteins from ΔrpoH mutant cells. Overall, our data showed that the S. intermedius DnaK chaperone system has important functions in quality control of cellular proteins but has less participation in the modulation of expression of pathogenic factors. (Keyword) Streptococci / molecular chaperone / 病原性 (Link to Publication Site) ● Publication site (DOI): 10.1007/s12192-011-0284-4 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21822788 ● Search Scopus @ Elsevier (PMID): 21822788 ● Search Scopus @ Elsevier (DOI): 10.1007/s12192-011-0284-4 (DOI: 10.1007/s12192-011-0284-4, PubMed: 21822788)
28.	Toshifumi Tomoyasu, Atsushi Tabata, Hiroshima Riki, Imaki Hidenori, Masuda Sachiko, Whiley A. Robert, Aduse-Opoku Joseph, Kikuchi Ken, Hiramatsu Keiichi and Hideaki Nagamune : Role of catabolite control protein A in the regulation of intermedilysin production by Streptococcus intermedius., Infection and Immunity, Vol.78, No.9, 4012-4021, 2010. (Summary) Streptococcus intermedius is an opportunistic pathogen of humans that causes purulent infections, including brain and liver abscesses. This pathogen secretes a human-specific cytolysin, intermedilysin, which has been recognized as a major virulence factor. However, most of the expressional control mechanisms of ily are still unknown. To determine these mechanisms, we analyzed the nucleotide sequence of the ily promoter region. We found a highly homologous region to the catabolite-repressible element (cre) in the ily promoter region and observed a considerable decrease in the amount of secreted intermedilysin when cells were grown in a culture medium containing high concentrations of glucose/utilizable carbohydrates. Disruption of the ccpA gene, which encodes catabolite control protein A, did not induce catabolite repression of ily by glucose/utilizable carbohydrates. In cre mutants, catabolite repression of ily was partially restored, and purified catabolite control protein A bound to an oligonucleotide containing the cre consensus sequence in the ily promoter region. In addition, a prolonged lag phase and slower doubling time of the ccpA mutant cells were observed. Our data show that S. intermedius can modulate ily expression and growth rate through catabolite control protein A-mediated monitoring of the extracellular glucose/utilizable carbohydrate concentration. (Keyword) virulence factor (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.00113-10 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20624907 ● Search Scopus @ Elsevier (PMID): 20624907 ● Search Scopus @ Elsevier (DOI): 10.1128/IAI.00113-10 (DOI: 10.1128/IAI.00113-10, PubMed: 20624907)
29.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Investigation of the chaperone function of the small heat shock protein AgsA., BMC Biochemistry, Vol.11, 27, 2010. (Summary) A small heat shock protein AgsA was originally isolated from Salmonella enterica serovar Typhimurium. We previously demonstrated that AgsA was an effective chaperone that could reduce the amount of heat-aggregated proteins in an Escherichia coli rpoH mutant. AgsA appeared to promote survival at lethal temperatures by cooperating with other chaperones in vivo. To investigate the aggregation prevention mechanisms of AgsA, we constructed N- or C-terminal truncated mutants and compared their properties with wild type AgsA. AgsA showed significant overall homology to wheat sHsp16.9 allowing its three-dimensional structure to be predicted. Truncations of AgsA until the N-terminal 23rd and C-terminal 11th amino acid (AA) from both termini preserved its in vivo chaperone activity. Temperature-controlled gel filtration chromatography showed that purified AgsA could maintain large oligomeric complexes up to 50 degrees C. Destabilization of oligomeric complexes was observed for N-terminal 11- and 17-AA truncated AgsA; C-terminal 11-AA truncated AgsA could not form large oligomeric complexes. AgsA prevented the aggregation of denatured lysozyme, malate dehydrogenase (MDH) and citrate synthase (CS) but did not prevent the aggregation of insulin at 25 degrees C. N-terminal 17-AA truncated AgsA showed no chaperone activity towards MDH. C-terminal 11-AA truncated AgsA showed weak or no chaperone activity towards lysozyme, MDH and CS although it prevented the aggregation of insulin at 25 degrees C. When the same amount of AgsA and C-terminal 11-AA truncated AgsA were mixed (half of respective amount required for efficient chaperone activities), good chaperone activity for all substrates and temperatures was observed. Detectable intermolecular exchanges between AgsA oligomers at 25 degrees C were not observed using fluorescence resonance energy transfer analysis; however, significant exchanges between AgsA oligomers and C-terminal truncated AgsA were observed at 25 degrees C. Our data demonstrate that AgsA has several regions necessary for efficient chaperone activity: region(s) important for lysozyme chaperone activity are located outer surface of the oligomeric complex while those region(s) important for insulin are located inside the oligomeric complex and those for MDH are located within the N-terminal arm. In addition, the equilibrium between the oligomer and the dimer structures appears to be important for its efficient chaperone activity. (Keyword) chaperone (Tokushima University Institutional Repository) ● Metadata: 114744 (Link to Publication Site) ● Publication site (DOI): 10.1186/1471-2091-11-27 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20653971 ● Search Scopus @ Elsevier (PMID): 20653971 ● Search Scopus @ Elsevier (DOI): 10.1186/1471-2091-11-27 (Tokushima University Institutional Repository: 114744, DOI: 10.1186/1471-2091-11-27, PubMed: 20653971)
30.	A de Marco, E. Deuerling, A. Mogk, Toshifumi Tomoyasu and B. Bukau : Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli., BMC Biotechnology, Vol.7, No.32, 2007. (Summary) BACKGROUND: The overproduction of recombinant proteins in host cells often leads to their misfolding and aggregation. Previous attempts to increase the solubility of recombinant proteins by co-overproduction of individual chaperones were only partially successful. We now assessed the effects of combined overproduction of the functionally cooperating chaperone network of the E. coli cytosol on the solubility of recombinant proteins. RESULTS: A two-step procedure was found to show the strongest enhancement of solubility. In a first step, the four chaperone systems GroEL/GroES, DnaK/DnaJ/GrpE, ClpB and the small HSPs IbpA/IbpB, were coordinately co-overproduced with recombinant proteins to optimize de novo folding. In a second step, protein biosynthesis was inhibited to permit chaperone mediated refolding of misfolded and aggregated proteins in vivo. This novel strategy increased the solubility of 70% of 64 different heterologous proteins tested up to 42-fold. CONCLUSION: The engineered E. coli strains and the two-step procedure presented here led to a remarkable increase in the solubility of a various recombinant proteins and should be applicable to a wide range of target proteins produced in biotechnology. (Keyword) Chaperone / Inclusion body / recombinant proteins / solbilization (Link to Publication Site) ● Publication site (DOI): 10.1186/1472-6750-7-32 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17565681 ● Search Scopus @ Elsevier (PMID): 17565681 ● Search Scopus @ Elsevier (DOI): 10.1186/1472-6750-7-32 (DOI: 10.1186/1472-6750-7-32, PubMed: 17565681)
31.	Akiko Takaya, Mari Matsui, Toshifumi Tomoyasu, Michihiro Kaya and Tomoko Yamamoto : The DnaK chaperone machinery converts the native FlhD₂C₂ hetero-tetramer into a functional transcriptional regulator of flagellar regulon expression in Salmonella., Molecular Microbiology, Vol.59, No.4, 1327-1340, 2006. (Summary) The DnaK chaperone binds non-specifically to many unfolded polypeptides and also binds selectively to specific substrates. Although its involvement in targeting the unfolded polypeptides to assist proper folding is well documented, less is known about its role in targeting the folded polypeptides. We demonstrate that DnaK regulates the expression of the Salmonella flagellar regulon by modulating the FlhD and FlhC proteins, which function as master regulators at the apex of a transcription hierarchy comprising three classes of genes. FlhD and FlhC form an FlhD2C2 complex that activates sigma70 promoter of class 2 genes. In DeltadnaK cells, FlhD and FlhC proteins seemed to be assembled into hetero-tetrameric FlhD2C2 but the complex was not fully active in class 2 gene transcription, suggesting that the DnaK chaperone is involved in activating native FlhD2C2 complex into a regulator of flagellar regulon expression. This is the first time that involvement of the DnaK chaperone machinery in activating folded oligomerized proteins has been demonstrated. (Keyword) Bacterial Proteins / Flagella / Gene Deletion / Gene Expression Regulation, Bacterial / Molecular Chaperones / Mutation / Protein Folding / Salmonella typhimurium / Trans-Activators / Transcription, Genetic (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1365-2958.2005.05016.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16430704 ● Search Scopus @ Elsevier (PMID): 16430704 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1365-2958.2005.05016.x (DOI: 10.1111/j.1365-2958.2005.05016.x, PubMed: 16430704)
32.	Toshifumi Tomoyasu, A Takaya, Y Handa, K Karata and T Yamamoto : ClpXP controls the expression of LEE genes in enterohaemorrhagic Escherichia coli., FEMS Microbiology Letters, Vol.253, No.1, 59-66, 2005. (Summary) Enterohaemorrhagic Escherichia coli (EHEC) contains a 36-kb pathogenicity island termed the locus of enterocyte effacement (LEE), which encodes a type III secretion system (TTSS) and virulence proteins. In this paper, we show that the O157:H7 Sakai clpPX mutant strongly impaired the secretion of virulence proteins by TTSS and repressed transcription from all the LEE promoters. The rpoS mutation in O157:H7 Sakai enhanced the transcription from all the LEE promoters and the secretion of virulence proteins, and it could partially suppress the defects of the clpPX mutation. These data indicate that the O157:H7 Sakai ClpXP protease is a positive regulator for LEE expression and that this regulation occurs by two pathways: the sigma(S)-dependent and -independent pathways. (Keyword) Bacterial Proteins / Base Sequence / DNA, Bacterial / Endopeptidase Clp / Escherichia coli O157 / Escherichia coli Proteins / Gene Expression Regulation, Bacterial / Genes, Bacterial / Genomic Islands / Humans / Mutation / Phosphoproteins / Sigma Factor / Virulence (Link to Publication Site) ● Publication site (DOI): 10.1016/j.femsle.2005.09.020 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16213673 ● Search Scopus @ Elsevier (PMID): 16213673 ● Search Scopus @ Elsevier (DOI): 10.1016/j.femsle.2005.09.020 (DOI: 10.1016/j.femsle.2005.09.020, PubMed: 16213673)
33.	A Takaya, A Suzuki, Y Kikuchi, M Eguchi, E Isogai, Toshifumi Tomoyasu and T Yamamoto : Derepression of Salmonella pathogenicity island 1 genes within macrophages leads to rapid apoptosis via caspase-1- and caspase-3-dependent pathways., Cellular Microbiology, Vol.7, No.1, 79-90, 2005. (Summary) Salmonella enterica serovar Typhimurium has been reported to induce apoptosis in infected macrophages within 14 h from the time of infection by a caspase-1-dependent mechanism. Here, we demonstrate that depletion of Lon protease in serovar Typhimurium induces rapid and massive apoptosis in macrophages by a mechanism involving both caspases-1 and -3. This excessive induction of apoptosis was abrogated by disruption of invF, which is required for the expression of the Salmonella pathogenicity island 1 (SPI1) genes. Expression of hilA, a central regulator of SPI1 transcription, was repressed in the macrophages after phagocytosis, but this gene was continuously expressed when the DeltaLon mutant grew within the macrophages, so the SPI1 proteins accumulated. Thus, the increase in macrophage apoptosis induced by the DeltaLon mutant could result from continued expression of SPI1 genes under conditions where they are normally repressed. Once Salmonella has established a systemic infection, excess apoptosis of macrophages cells upon which the organism is reliant would be detrimental to the pathogen. Therefore, the Lon protease may be required to suppress apoptosis sufficiently to allow time for the bacterium to replicate, escape and invade new macrophages. (Keyword) Animals / Apoptosis / Bacterial Proteins / Caspase 1 / Caspase 3 / Caspases / Cells, Cultured / DNA-Binding Proteins / Gene Expression Regulation, Bacterial / Genomic Islands / Macrophages / Mice / Mutation / Protease La / Salmonella typhimurium / Signal Transduction / Trans-Activators / Transcription Factors (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1462-5822.2004.00435.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15617525 ● Search Scopus @ Elsevier (PMID): 15617525 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1462-5822.2004.00435.x (DOI: 10.1111/j.1462-5822.2004.00435.x, PubMed: 15617525)
34.	A Takaya, Toshifumi Tomoyasu, H Matsui and T Yamamoto : The DnaK/DnaJ chaperone machinery of Salmonella enterica serovar Typhimurium is essential for invasion of epithelial cells and survival within macrophages, leading to systemic infection., Infection and Immunity, Vol.72, No.3, 1364-1373, 2004. (Summary) Salmonella enterica serovar Typhimurium, similar to various facultative intracellular pathogens, has been shown to respond to the hostile conditions inside macrophages of the host organism by inducing stress proteins, such as DnaK. DnaK forms a chaperone machinery with the cochaperones DnaJ and GrpE. To elucidate the role of the DnaK chaperone machinery in the pathogenesis of S. enterica serovar Typhimurium, we first constructed an insertional mutation in the dnaK-dnaJ operon of pathogenic strain chi3306. The DnaK/DnaJ-depleted mutant was temperature sensitive for growth, that is, nonviable above 39 degrees C. We then isolated a spontaneously occurring revertant of the dnaK-dnaJ-disrupted mutant at 39 degrees C and used it for infection of mice. The mutant lost the ability to cause a lethal systemic disease in mice. The impaired ability for virulence was restored when a functional copy of the dnaK-dnaJ operon was provided, suggesting that the DnaK/DnaJ chaperone machinery is required by Salmonella for the systemic infection of mice. This result also indicates that with respect to the DnaK/DnaJ chaperone machinery, the cellular requirements for growth at a high temperature are not identical to the cellular requirements for the pathogenesis of Salmonella. Macrophage survival assays revealed that the DnaK/DnaJ-depleted mutant could not survive or proliferate at all within macrophages. Of further interest are the findings that the mutant could neither invade cultured epithelial cells nor secrete any of the invasion proteins encoded within Salmonella pathogenicity island 1. This is the first time that the DnaK/DnaJ chaperone machinery has been shown to be involved in bacterial invasion of epithelial cells. (Keyword) Hsp70 / Salmonella / epithelial cells / infection (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.72.3.1364-1373.2004 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14977940 ● Search Scopus @ Elsevier (PMID): 14977940 ● Search Scopus @ Elsevier (DOI): 10.1128/IAI.72.3.1364-1373.2004 (DOI: 10.1128/IAI.72.3.1364-1373.2004, PubMed: 14977940)
35.	Toshifumi Tomoyasu, A Takaya, T Sasaki, R Kikuno, T Nagase, M Morioka and T Yamamoto : A new heat-shock gene agsA, which encodes a small chaperone involved in suppressing protein aggregation in Salmonella entrica serovar Typhimurium., Journal of Bacteriology, Vol.185, No.21, 6331-6339, 2003. (Keyword) molecular chaperone / small heat shock protein / protein aggregation
36.	Y Yamaguchi, Toshifumi Tomoyasu, A Takaya, M Morioka and T Yamamoto : Effects of disruption of heat shock genes on susceptibility of Escherichia coli to fluoroquinolones., BMC Microbiology, Vol.3, No.1, 16, 2003. (Summary) It is well known that expression of certain bacterial genes responds rapidly to such stimuli as exposure to toxic chemicals and physical agents. It is generally believed that the proteins encoded in these genes are important for successful survival of the organism under the hostile conditions. Analogously, the proteins induced in bacterial cells exposed to antibiotics are believed to affect the organisms' susceptibility to these agents. We demonstrated that Escherichia coli cells exposed to levofloxacin (LVFX), a fluoroquinolone (FQ), induce the syntheses of heat shock proteins and RecA. To examine whether the heat shock proteins affect the bactericidal action of FQs, we constructed E. coli strains with mutations in various heat shock genes and tested their susceptibility to FQs. Mutations in dnaK, groEL, and lon increased this susceptibility; the lon mutant exhibited the greatest effects. The increased susceptibility of the lon mutant was corroborated by experiments in which the gene encoding the cell division inhibitor, SulA, was subsequently disrupted. SulA is induced by the SOS response and degraded by the Lon protease. The findings suggest that the hypersusceptibility of the lon mutant to FQs could be due to abnormally high levels of SulA protein resulting from the depletion of Lon and the continuous induction of the SOS response in the presence of FQs. The present results show that the bactericidal action of FQs is moderately affected by the DnaK and GroEL chaperones and strongly affected by the Lon protease. FQs have contributed successfully to the treatment of various bacterial infections, but their widespread use and often misuse, coupled with emerging resistance, have gradually compromised their utility. Our results suggest that agents capable of inhibiting the Lon protease have potential for combination therapy with FQs. (Keyword) heat shock / quinolones / Escherichia coli (Link to Publication Site) ● Publication site (DOI): 10.1186/1471-2180-3-16 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12911840 ● Search Scopus @ Elsevier (PMID): 12911840 ● Search Scopus @ Elsevier (DOI): 10.1186/1471-2180-3-16 (DOI: 10.1186/1471-2180-3-16, PubMed: 12911840)
37.	Toshifumi Tomoyasu, A Takaya, E Isogai and T Yamamoto : Turnover of FlhD and FlhC, master regulator proteins for Salmonella flagellum biogenesis, by the ATP-dependent ClpXP protease., Molecular Microbiology, Vol.48, No.2, 443-452, 2003. (Summary) In enterobacteria such as Salmonella, flagellar biogenesis is dependent upon the master operon flhDC at the apex of the flagellar gene hierarchy, which is divided into three classes 1, 2 and 3. Previously we reported that depletion of the ClpXP ATP-dependent protease results in dramatic enhancement of class 2 and class 3 gene transcription, whereas the transcription level of the flhDC operon remains normal in Salmonella enterica serovar Typhimurium. This suggests that the ClpXP protease may be responsible for the turnover of the FlhD and FlhC master regulators (Tomoyasu, T., Ohkishi, T., Ukyo, Y., Tokumitsu, A., Takaya, A., Suzuki, M. et al., 2002, J Bacteriol 184:645-653). In this study, to establish the role of the ClpXP protease in the turnover of FlhD and FlhC proteins, we analysed levels of the FlhD and FlhC proteins in wild-type and ClpXP mutant cells using anti-FlhD and anti-FlhC antibodies. The results show that both FlhD and FlhC proteins are markedly accumulated in ClpXP mutant cells and the half-life of FlhC is approximately fivefold longer in the ClpXP mutant, suggesting that the ClpXP protease is responsible for the degradation of FlhD and FlhC. The results also show that the ClpXP protease degrades both proteins in FlhD2FlhC2 complex but does not seem to recognize the respective subunits synthesized individually. Taken together, it is suggested that the cellular concentration of the FlhD2FlhC2 master regulator is tightly controlled at the post-translational level by the ClpXP protease. We also examined the role of other members of the ATP-dependent protease family in the regulation of flagellar biogenesis and concluded that only ClpXP in this family functions as a negative regulator for flagellar biogenesis in Salmonella. (Keyword) Salmonella / flagellum / ClpXP protease / FlhD / FlhC (Link to Publication Site) ● Publication site (DOI): 10.1046/j.1365-2958.2003.03437.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12675803 ● Search Scopus @ Elsevier (PMID): 12675803 ● Search Scopus @ Elsevier (DOI): 10.1046/j.1365-2958.2003.03437.x (DOI: 10.1046/j.1365-2958.2003.03437.x, PubMed: 12675803)
38.	A Takaya, M Suzuki, H Matsui, Toshifumi Tomoyasu, H Sashinami, A Nakane and T Yamamoto : Lon, a stress-induced ATP-dependent protease is critically important for the systemic Salmonella infection of mice., Infection and Immunity, Vol.71, No.2, 690-696, 2003. (Summary) Studies on the pathogenesis of Salmonella enterica serovar Typhimurium infections in mice have revealed the presence of two prominent virulence characteristics-the invasion of the nonphagocytic cells to penetrate the intestinal epithelium and the proliferation within host phagocytic cells to cause a systemic spread and the colonization of host organs. We have recently demonstrated that the ATP-dependent Lon protease of S. enterica serovar Typhimurium negatively regulates the efficiency of invasion of epithelial cells and the expression of invasion genes (A. Takaya et al., J. Bacteriol. 184:224-232, 2002). This study was performed to reveal the contribution of the Lon protease to the virulence of S. enterica serovar Typhimurium in mice. Determination of 50% lethal doses for the lon disruption mutant and wild-type strain revealed that the mutant was highly attenuated when administered either orally or intraperitoneally to BALB/c mice. The mutant was also found to be able to reach extraintestinal sites but unable to proliferate efficiently within the spleen and cause lethal systemic disease of mice. Macrophage survival assays revealed that the lon disruption mutant could not survive or proliferate within murine macrophages. In addition, the mutant showed extremely increased susceptibility to hydrogen peroxide, which contributes to the bactericidal capacity of phagocytes. The mutant also showed increased sensitivity to acidic conditions. Taken together, the impaired ability of the lon disruption mutant to survive and grow in macrophages could be due to the enhanced susceptibility to the oxygen-dependent killing mechanism associated with respiratory burst and the low phagosomal pH. These results suggest that the Lon protease is essentially involved in the systemic infection of mice with S. enterica serovar Typhimurium, which can be fatal. Of further interest is the finding that the lon disruption mutant persists in the BALB/c mice for long periods without causing an overwhelming systemic infection. (Keyword) Salmonella / infection / Lon protease / infection / mice (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.71.2.690-696.2003 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12540547 ● Search Scopus @ Elsevier (PMID): 12540547 ● Search Scopus @ Elsevier (DOI): 10.1128/IAI.71.2.690-696.2003 (DOI: 10.1128/IAI.71.2.690-696.2003, PubMed: 12540547)
39.	H Matsui, M Suzuki, Y Isshiki, M Eguchi, Y Kikuchi, K Motokawa, A Takaya, Toshifumi Tomoyasu and T Yamamoto : Oral immunization with ATP-dependent protease-deficient mutants protects mice against subsequent oral challenge with virulent Salmonella enterica serovar typhimurium., Infection and Immunity, Vol.71, No.1, 30-39, 2003. (Summary) We evaluated the efficacy of mutants with a deletion of the stress response protease gene as candidates for live oral vaccine strains against Salmonella infection through infection studies with mice by using a Salmonella enterica serovar Typhimurium mutant with a disruption of the ClpXP or Lon protease. In vitro, the ClpXP protease regulates flagellum synthesis and the ClpXP-deficient mutant strain exhibits hyperflagellated bacterial cells (T. Tomoyasu et al., J. Bacteriol. 184:645-653, 2002). On the other hand, the Lon protease negatively regulates the efficacy of invading epithelial cells and the expression of invasion genes (A. Takaya et al., J. Bacteriol. 184:224-232, 2002). When 5-week-old BALB/c mice were orally administered 5 x 10(8) CFU of the ClpXP- or Lon-deficient strain, bacteria were detected with 10(3) to 10(4) CFU in the spleen, mesenteric lymph nodes, Peyer's patches, and cecum 1 week after inoculation and the bacteria then decreased gradually in each tissue. Significant increases of lipopolysaccharide-specific immunoglobulin G (IgG) and secretory IgA were detected at week 4 and maintained until at least week 12 after inoculation in serum and bile, respectively. Immunization with the ClpXP- or Lon-deficient strain protected mice against oral challenge with the serovar Typhimurium virulent strain. Both the challenged virulent and immunized avirulent salmonellae were completely cleared from the spleen, mesenteric lymph nodes, Peyer's patches, and even cecum 5 days after the challenge. These data indicate that Salmonella with a disruption of the ATP-dependent protease ClpXP or Lon can be useful in developing a live vaccine strain. (Keyword) Oral immunization / protease-deficient mutants / AAA protease / mice (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.71.1.30-39.2003 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12496146 ● Search Scopus @ Elsevier (PMID): 12496146 ● Search Scopus @ Elsevier (DOI): 10.1128/IAI.71.1.30-39.2003 (DOI: 10.1128/IAI.71.1.30-39.2003, PubMed: 12496146)
40.	Toshifumi Tomoyasu, T Ohkishi, Y Ukyo, A Tokumitsu, A Takaya, M Suzuki, K Sekiya, H Matsui, K Kutsukake and T Yamamoto : The ClpXP ATP-dependent protease regulates flagellum synthesis in Salmonella enterica serovar Typhimurium., Journal of Bacteriology, Vol.184, No.3, 645-653, 2002. (Keyword) Salmonella / ClpXP protease / flagellum / synthesis
41.	A Takaya, Toshifumi Tomoyasu, A Tokumitsu, M Morioka and T Yamamoto : The ATP-dependent Lon protease of Salmonella enterica serovar Typhimurium regulates invasion and expression of genes encoded on Salmonella pathogenicity island 1., Journal of Bacteriology, Vol.184, No.1, 224-232, 2002. (Keyword) Salmonella / Lon protease / pathogenicity island
42.	Toshifumi Tomoyasu, F Arsene, T Ogura and B Bukau : The C terminus of sigma32 is not essential for degradation by FtsH., Journal of Bacteriology, Vol.183, No.20, 5911-5917, 2001.
43.	T Yamamoto, H Sashinami, A Takaya, Toshifumi Tomoyasu, H Matsui, T Hanawa, S Kamiya and A Nakane : Disruption of the Genes for ClpXP Protease in Salmonella enterica Serovar Typhimurium Results in a Persistent Infection in Mouse and Development of the Persistence Requires Endogenous Gamma Interferon and Tumor Necrosis Factor Alpha., Infection and Immunity, Vol.69, No.5, 3164-3174, 2001. (Summary) The enteric pathogen Salmonella enterica serovar Typhimurium, similar to other facultative intracellular pathogens, has been shown to respond to the hostile conditions inside macrophages of the host organism by producing a set of stress proteins that are also induced by various environmental stresses. The stress-induced ClpXP protease is a member of the ATP-dependent proteases, which are known to be responsible for more than 90% of all proteolysis in Escherichia coli. To investigate the contribution of the ClpXP protease to the virulence of serovar Typhimurium we initially cloned the clpP and clpX operon from the pathogenic strain serovar Typhimurium chi3306 and then created insertional mutations in the clpP and/or clpX gene. The Delta clpP and Delta clpX mutants were used to inoculate BALB/c mice by either the intraperitoneal or the oral route and found to be limited in their ability to colonize organs of the lymphatic system and to cause systemic disease in the host. A variety of experiments were performed to determine the possible reasons for the loss of virulence. An oxygen-dependent killing assay using hydrogen peroxide and paraquat (a superoxide anion generator) and a serum killing assay using murine serum demonstrated that all of the serovar Typhimurium Delta clpP and Delta clpX mutants were as resistant to these killing mechanisms as the wild-type strain. On the other hand, the macrophage survival assay revealed that all these mutants were more sensitive to the intracellular environment than the wild-type strain and were unable to grow or survive within peritoneal macrophages of BALB/c mice. In addition, it was revealed that the serovar Typhimurium ClpXP-depleted mutant was not completely cleared but found to persist at low levels within spleens and livers of mice. Interferon gamma-deficient mice and tumor necrosis factor alpha-deficient mice failed to survive the attenuated serovar Typhimurium infections, suggesting that both endogenous cytokines are essential for regulation of persistent infection with serovar Typhimurium. (Keyword) Salmonella / ClpXP Protease / infection / Mouse / Persistence (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.69.5.3164-3174.2001 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11292737 ● Search Scopus @ Elsevier (PMID): 11292737 ● Search Scopus @ Elsevier (DOI): 10.1128/IAI.69.5.3164-3174.2001 (DOI: 10.1128/IAI.69.5.3164-3174.2001, PubMed: 11292737)
44.	Toshifumi Tomoyasu, A Mogk, H Langen, P Goloubinoff and B Bukau : Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol., Molecular Microbiology, Vol.40, No.2, 397-413, 2001. (Summary) We investigated the roles of chaperones and proteases in quality control of proteins in the Escherichia coli cytosol. In DeltarpoH mutants, which lack the heat shock transcription factor and therefore have low levels of all major cytosolic proteases and chaperones except GroEL and trigger factor, 5-10% and 20-30% of total protein aggregated at 30 degrees C and 42 degrees C respectively. The aggregates contained 350-400 protein species, of which 93 were identified by mass spectrometry. The aggregated protein species were similar at both temperatures, indicating that thermolabile proteins require folding assistance by chaperones already at 30 degrees C, and showed strong overlap with previously identified DnaK substrates. Overproduction of the DnaK system, or low-level production of the DnaK system and ClpB, prevented aggregation and provided thermotolerance to DeltarpoH mutants, indicating key roles for these chaperones in protein quality control and stress survival. In rpoH+ cells, DnaK depletion did not lead to protein aggregation at 30 degrees C, which is probably the result of high levels of proteases and thus suggests that DnaK is not a prerequisite for proteolysis of misfolded proteins. Lon was the most efficient protease in degrading misfolded proteins in DnaK-depleted cells. At 42 degrees C, ClpXP and Lon became essential for viability of cells with low DnaK levels, indicating synergistic action of proteases and the DnaK system, which is essential for cell growth at 42 degrees C. (Keyword) Escherichia coli / molecular chaperone / protease (Link to Publication Site) ● Publication site (DOI): 10.1046/j.1365-2958.2001.02383.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11309122 ● Search Scopus @ Elsevier (PMID): 11309122 ● Search Scopus @ Elsevier (DOI): 10.1046/j.1365-2958.2001.02383.x (DOI: 10.1046/j.1365-2958.2001.02383.x, PubMed: 11309122)
45.	A Mogk, Toshifumi Tomoyasu, P Goloubinoff, S Rudiger, D Roder, H Langen and B Bukau : Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB., The EMBO Journal, Vol.18, No.24, 6934-6949, 1999. (Keyword) Escherichia coli / protein / aggregation / DnaK / ClpB
46.	P Goloubinoff, A Mogk, AP Zvi, Toshifumi Tomoyasu and B Bukau : Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network., Proceedings of the National Academy of Sciences of the United States of America, Vol.96, No.24, 13732-13737, 1999. (Keyword) Escherichia coli / refolding / solubilization / protein aggregates / ClpB
47.	E Deuerling, A Schulze-Specking, Toshifumi Tomoyasu, A Mogk and B Bukau : Trigger factor and DnaK cooperate in folding of newly synthesized proteins., Nature, Vol.400, No.6745, 693-696, 1999. (Keyword) Escherichia coli / Trigger factor / DnaK / newly synthesized proteins
48.	F Arsene, Toshifumi Tomoyasu, A Mogk, C Schirra, A Schulze-Specking and B Bukau : Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32, Journal of Bacteriology, Vol.181, No.11, 3552-3561, 1999. (Keyword) Escherichia coli / sigma32 / heat shock / region C
49.	T Tatsuta, Toshifumi Tomoyasu, B Bukau, M Kitagawa, H Mori, K Karata and T Ogura : Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity control mechanisms of sigma32 in vivo., Molecular Microbiology, Vol.30, No.3, 833-844, 1999. (Keyword) Escherichia coli / heat shock / transcription factor / RpoH
50.	T Ogura, K Inoue, T Tatsuta, T Suzaki, K Karata, K Young, LH Su, CA Fierke, JE Jackman, CR Raetz, J Coleman, Toshifumi Tomoyasu and H Matsuzawa : Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli., Molecular Microbiology, Vol.31, No.3, 833-844, 1999. (Keyword) Escherichia coli / AAA protease / FtsH / lipid
51.	Toshifumi Tomoyasu, T Ogura, T Tatsuta and B Bukau : Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli., Molecular Microbiology, Vol.30, No.3, 567-581, 1998. (Keyword) Escherichia coli / heat shock / DnaK / DnaJ / protein repair
52.	S Cutting, M Anderson, E Lysenko, A Page, Toshifumi Tomoyasu, K Tatematsu, T Tatsuta, L Kroos and T Ogura : SpoVM, a small protein essential to development in Bacillus subtilis, interacts with the ATP-dependent protease FtsH., Journal of Bacteriology, Vol.179, No.17, 5534-5542, 1997. (Keyword) Bacillus subtilis / Sporulation / SpoVM / FtsH
53.	Y Shotland, S Koby, D Teff, N Mansur, DA Oren, K Tatematsu, Toshifumi Tomoyasu, M Kessel, B Bukau, T Ogura and AB Oppenheim : Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli., Molecular Microbiology, Vol.24, No.6, 1303-1310, 1997. (Keyword) Escherichia coli / FtsH / lambda phage / CII
54.	JN Qu, SI Makino, H Adachi, Y Koyama, Y Akiyama, K Ito, Toshifumi Tomoyasu, T Ogura and H Matsuzawa : The tolZ gene of Escherichia coli is identified as the ftsH gene., Journal of Bacteriology, Vol.178, No.12, 3457-3461, 1996. (Keyword) Escherichia coli / FtsH / colicin / tolerant
55.	J Gamer, G Multhaup, Toshifumi Tomoyasu, JS McCarty, S Rudiger, HJ Schonfeld, C Schirra, H Bujard and B Bukau : A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32., The EMBO Journal, Vol.15, No.3, 607-617, 1996.
56.	Toshifumi Tomoyasu, J Gamer, B Bukau, M Kanemori, H Mori, AJ Rutman, AB Oppenheim, T Yura, K Yamanaka, H Niki, S Hiraga and T Ogura : Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma32., The EMBO Journal, Vol.14, No.11, 2551-2560, 1995. (Keyword) Escherichia coli / heat shock / transcription factor / Sigma32 / FtsH
57.	D Nilsson, AA Lauridsen, Toshifumi Tomoyasu and T Ogura : A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product., Microbiology, Vol.140, No.10, 2601-2610, 1994. (Keyword) Lactococcus lactis / Escherichia coli / protease / FtsH
58.	C Herman, T Ogura, Toshifumi Tomoyasu, S Hiraga, Y Akiyama, K Ito, R Thomas, R D'Ari and P Bouloc : Cell growth and lambda phage development controlled by the same essential Escherichia coli gene, ftsH/hflB., Proceedings of the National Academy of Sciences of the United States of America, Vol.90, No.22, 10861-10865, 1993. (Keyword) Escherichia coli / lambda phage / FtsH / protease
59.	Toshifumi Tomoyasu, T Yuki, S Morimura, H Mori, K Yamanaka, H Niki, S Hiraga and T Ogura : The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression., Journal of Bacteriology, Vol.175, No.5, 1344-1351, 1993. (Keyword) Escherichia coli / AAA family / FtsH / p97/VCP homologue
60.	Toshifumi Tomoyasu, K Yamanaka, K Murata, T Suzaki, P Bouloc, A Kato, H Niki, S Hiraga and T Ogura : Topology and subcellular localization of FtsH protein in Escherichia coli., Journal of Bacteriology, Vol.175, No.5, 1352-1357, 1993. (Keyword) Escherichia coli / topology / localization / FtsH / protease
61.	KJ Begg, Toshifumi Tomoyasu, WD Donachie, M Khattar, H Niki, K Yamanaka, S Hiraga and T Ogura : Escherichia coli mutant Y16 is a double mutant carrying thermosensitive ftsH and ftsI mutations., Journal of Bacteriology, Vol.174, No.7, 2416-2417, 1992. (Keyword) Escherichia coli / filamentation / FtsH / FtsI / thermo-sensitive mutation
62.	H Tohoyama, Toshifumi Tomoyasu, M Inouhe, M Joho and T Murayama : The gene for cadmium metallothionein from a cadmium-resistant yeast appears to be identical to CUP1 in a copper-resistant strain., Current Genetics, Vol.21, No.4-5, 275-280, 1992. (Keyword) Saccharomyces cerevisiae / cadmium / metallothionein / resistant / CUP1
63.	T Ogura, Toshifumi Tomoyasu, T Yuki, S Morimura, KJ Begg, WD Donachie, H Mori, H Niki and S Hiraga : Structure and function of the ftsH gene in Escherichia coli., Research in Microbiology, Vol.142, No.2-3, 279-282, 1991. (Keyword) Escherichia coli / VCP / homologue / membrane protein

Review, Commentary:

1.	Toshifumi Tomoyasu and Hideaki Nagamune : Functional comparison between the DnaK chaperone systems of Streptococcus intermedius and Escherichia coli, STRESS AND ENVIRONMENTAL REGULATION OF GENE EXPRESSION AND ADAPTATION IN BACTERIA, Vol.2, 791-795, Jun. 2016. (Keyword) Streptococcus / Escherichia coli / molecular chaperone (Link to Publication Site) ● Publication site (DOI): 10.1002/9781119004813.ch76 (Link to Search Site for Scientific Articles) ● Summary page in Scopus @ Elsevier: 2-s2.0-85018833367 (DOI: 10.1002/9781119004813.ch76, Elsevier: Scopus)
2.	Toshifumi Tomoyasu : 大腸菌のトリガーファクター, Nihon Saikingaku Zasshi, Vol.57, No.4, 597-605, Nov. 2002. (Keyword) Escherichia coli / 新生タンパク質 / 折りたたみ / molecular chaperone / トリガーファクター
3.	MP Mayer, Toshifumi Tomoyasu and B Bukau : Hsp70シャペロンの分子メカニズム, 蛋白質核酸酵素, Vol.47, No.9, 1189-1195, Jul. 2002. (Keyword) molecular chaperone / Hsp70 / DnaJ / GepE
4.	F Arsène, Toshifumi Tomoyasu and B Bukau : The heat shock response of Escherichia coli., International Journal of Food Microbiology, Vol.55, No.1-3, 3-9, Apr. 2000. (Keyword) Escherichia coli / heat shock / transcription factor / molecular chaperone / protease
5.	小椋光, 多賀谷光男, Toshifumi Tomoyasu, 伊藤維昭, 秋山芳展, 中井俊樹, 大隅隆 and 塚本利朗 : AAAスーパーファミリータンパク質 - 新しいATPaseファミリーの構造とその多様な機能, 細胞工学, Vol.15, No.7, 968-979, Jul. 1996. (Keyword) AAAスーパーファミリー / ATPase / structure / function

Proceeding of International Conference:

1.	Yamada Takuya, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Response of human cells against peptide type hemolysin Streptolysin S derived from Streptococcus anginosus subsp. anginosus, International Peptide Symposium, Dec. 2018. (Keyword) Streptococcus / cytolysin / peptide
2.	Tang Qing, Masayoshi Onitsuka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Characterizatio of anti-HER2 scFv and Fab as a targeting module for novel drug-delivery system against HER2-positive cancer, 24th IUBMB congress & 15th FAOBMB congress, Seoul, Korea, Jun. 2018.
3.	Toshifumi Tomoyasu, Atsushi Tabata, Chiba Shinya, Yamasaki Takahiro, Kusaka Shingo, Takeda Nozomi, Tamaoka Masaaki, Kazuto Ohkura, Whiley A. Robert and Hideaki Nagamune : Positive and negative control mechanisms of pathogenicity expression in Streptococcus intermedius, Lancefield International Symposium on Streptococci and Streptococcal Diseases, Denarau Island Fiji, Oct. 2017. (Keyword) pathogenic microorganism / bacterial toxins / immunity
4.	Atsushi Tabata, Deutsch Douglas, Otsuka Seiya, Verratti Kathleen, Toshifumi Tomoyasu, Hideaki Nagamune and Fischetti A. Vincent : Characterization of a novel plasmid discovered in a clinical isolate of Streptococcus anginosus subsp. anginosus, Lancefield International Symposium on Streptococci and Streptococcal Diseases, Denarau Island Fiji, Oct. 2017. (Keyword) pathogenic microorganism / plasmid
5.	Toshifumi Tomoyasu, Shinya Chiba, Takahiro Yamasaki, Shingo Kusaka, Atsushi Tabata and Hideaki Nagamune : Expression control pathways of ily by blood components in Streptococcus intermedius, The 13th Korea - Japan International Symposium on Microbiology (XIII-KJISM), May 2016. (Keyword) cytolysin / sugar / antibody / Streptococcus
6.	Hideaki Nagamune, Toshifumi Tomoyasu, Hidenori Imaki, Naoki Yamamoto, Chiharu Taue, 増田早智子, 高尾亞由子, 前田伸子, Atsushi Tabata and Whiley A. Robert : CHARACTERIZATION OF A NOVEL SECRETED GLYCOSIDASE WITH MULTIPLE GLYCOSIDASE ACTIVITIES, MSGA: A CANDIDATE KEY ENZYME REGULATING GROWTH AND PATHOGENICITY OF STREPTOCOCCUS INTERMEDIUS, XIX Lancefield International Symposium on Streptococci and Streptococcal Diseases, Nov. 2014. (Keyword) Streptococcus / enzyme / gene expression / cytolysin
7.	Atsushi Tabata, Kota Nakano, Yuji Sato, Kentaro Maya, Hiromi Ohtani, Yukimasa Ohkubo, Kazuto Ohkura, Ken Kikuchi, Robert A Whiley, Toshifumi Tomoyasu and Hideaki Nagamune : STREPTOLYSIN S HOMOLOGUES OF PEPTIDE HEMOLYSIN: NOVEL BETA-HEMOLYTIC FACTORS DISTRIBUTED AMONG BETA-HEMOLYTIC ANGINOSUS GROUP STREPTOCOCCI, XIX Lancefield International Symposium on Streptococci and Streptococcal Diseases, Buenos Aires, Argentina, Nov. 2014. (Keyword) Streptococcus / pathogenic microorganism / virulence factor
8.	Aya Miyazaki, Keigo Tsuruno, Toshifumi Tomoyasu and Kenji Sonomoto : Functional analysis of Streptococcus intermedius DnaK system in vitro, The 8th International AFAS Joint Symposium Between Japan and Korea, Tottori, Japan, Nov. 2011. (Keyword) Streptococci / molecular chaperone / protein
9.	Yukihiro Nishikawa, Atsushi Tabata, Toshifumi Tomoyasu, Momoyo Azuma, Yasuhiko Nishioka, Saburo Sone and Hideaki Nagamune : Triple fusion PCR immunochromatography for a rapid and simple diagnosis of penicillin-resistant Streptococcus pneumoniae, IUMS 2011 Sapporo Congress, Sapporo, Japan, Sep. 2011. (Keyword) Streptococci / antibiotics / clinical laboratory testing
10.	Kota Nakano, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Investigation of the novel cytotoxic factor secreted from streptococcus anginosus, IUMS 2011 Sapporo Congress, Sapporo, Sep. 2011.
11.	Hidenori Imaki, Toshifumi Tomoyasu, Sachiko Masuda, Atsushi Tabata and Hideaki Nagamune : Molecular and phenotypic analysis of mutants of ily expressional control factors in Streptococcus intermedius, IUMS 2011 Sapporo Congress, Palermo, Italy, Sep. 2011. (Keyword) Streptococci / cytolysin / gene expression
12.	Atsushi Tabata, Yasuhiro Yamamoto, Ayuko Takao, Toshifumi Tomoyasu, Ayako Nakayama, Nobuko Maeda, Hisashi Ohkuni and Hideaki Nagamune : Investigation of pathogenic properties of cholesterol-dependent cytolysin producing Streptococcus mitis, XVIII Lancefield International Symposium, Palermo, Italy, Sep. 2011. (Keyword) Streptococci / cytolysin
13.	Toshifumi Tomoyasu, Sachiko Masuda, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : Genetic screening of ily expression control factors in Streptococcus intermedius, XVIII Lancefield International Symposium, Palermo, Italy, Sep. 2011. (Keyword) Streptococci / cytolysin / gene expression
14.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Functions of DnaK chaperone system in Streptococcus intermedius, Cell Stress Society International, Sapporo, Oct. 2009. (Keyword) pathogenic microorganism / virulence factor
15.	Atsushi Tabata, Shizuka Saito, Eriko Sakakura, Yuki Shinohara, Soichiro Miyoshi, Kou Fukushima, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : Streptococcus mitis-derived human platelet aggregation factor is a novel type of cholesterol-dependent cytolysin that recognizes dual receptors, cholesterol and human CD59., XVII Lancefield International Symposium on Streptococci & Streptococcal Diseases, Porto Heli, Greece, Jun. 2008.
16.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Function of DnaK in Streptococcus intermedius, Cell Stress Society International, Budapest, Aug. 2007. (Keyword) Streptococcus / Chaperon / DnaK
17.	Atsushi Tabata, Akiko Inubushi, Toshifumi Tomoyasu and Hideaki Nagamune : Immunochemical analysis of a human specific cytolysin, intermedilysin, for elucidation of its mode of action to human cells, 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
18.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Small heat shock protein ``AgsA'' suppresses aggregation of heat denatured proteins., 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
19.	Toshifumi Tomoyasu, Akiko Takaya and Yamamoto Tomoko : ClpXP and Lon proteases control the expression of LEE genes in enterohaemorrhagic Escherichia coli., CSH Meeting on Microbial pathogenesis & Host response, New York, Sep. 2005.

Proceeding of Domestic Conference:

1.	YAMAMORI Yugo, Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Streptococcus anginosusが産生するStreptolysin Sに対する宿主細胞応答のメカニズム, 第96回日本生化学会大会, Nov. 2023. (Keyword) レンサ球菌 / cytolysin
2.	AOYAMA Rina, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が保有する新規細胞壁アンカータンパク質の機能解析, 第76回日本細菌学会支部総会, Oct. 2023. (Keyword) レンサ球菌 / extracellular matrix
3.	Atsushi Tabata, YOKOHATA Shuto, Kazuto Ohkura, Toshifumi Tomoyasu and Hideaki Nagamune : レンサ球菌が産生するペプチド溶血毒素ストレプトリジンSの血清アルブミンによる活性保護, 第69回トキシンシンポジウム, Sep. 2023. (Keyword) レンサ球菌 / cytolysin
4.	YAMAMORI Yugo, Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Streptococcus anginosus が産生する Streptolysin S に対する宿主細胞応答のメカニズム, 第69回トキシンシンポジウム, Sep. 2023. (Keyword) レンサ球菌 / cytolysin / 宿主細胞応答
5.	OHOKA Keichiroh, Atsushi Tabata, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : Induction of cytokine gene expression in human cell line depending on N-terminal domain of Sm-hPAF, 第96回日本細菌学会総会, Mar. 2023. (Keyword) レンサ球菌 / ヒト血小板凝集因子 / cytolysin / 細胞応答
6.	YOKOHATA Shuto, Kazuto Ohkura, Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Human serum albumin stabilizes streptolysin S secreted by streptolysin S-producing streptococci, 第96回日本細菌学会総会, Mar. 2023. (Keyword) ヒト血清アルブミン / 細胞傷害 / cytolysin
7.	OKAMOTO Ryota, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Functional analysis of DnaK chaperone system in Brevibacillus brevis, 第96回日本細菌学会総会, Mar. 2023. (Keyword) Brevibacillus / molecular chaperone / DnaK / グラム陽性菌
8.	Atsushi Tabata, Airi Matsumoto, Ai Fujimoto, Toshifumi Tomoyasu, 髙尾亜由子, Hisashi Ohkuni and Hideaki Nagamune : Molecular characteristics of novel 5-domain type cholesterol-dependent cytolysin, discoidinolysin, 第96回日本細菌学会総会, Mar. 2023. (Keyword) レンサ球菌 / cytolysin / 分子特性
9.	YAMAMORI Yugo, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Mechanism of cellular response to Streptolysin S produced by Streptococcus anginosus, 第96回日本細菌学会総会, Mar. 2023. (Keyword) レンサ球菌 / cytolysin / 細胞応答
10.	TAKESHITA Ryoya, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 肺がん細胞指向性DDS ツールの作製に向けたリガンド分子の構築, 第146回徳島生物学会, Jan. 2023. (Keyword) 肺がん / DDS ツール / cancer therapy
11.	TAKEZAWA Kohji, Atsushi Tabata, Hideaki Nagamune and Toshifumi Tomoyasu : Development and evaluation of a novel micelle-based DDS tool for cancer therapy, 第95回日本生化学会大会, Nov. 2022. (Keyword) ミセル / DDS / cancer therapy
12.	Atsushi Tabata, Airi Matsumoto, Ai Fujimoto, IKEDA Takuya, Toshifumi Tomoyasu, 髙尾亜由子, Hisashi Ohkuni and Hideaki Nagamune : Streptococcus mitisが産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の分子特性と病原性への寄与, 第52回レンサ球菌研究会, Jul. 2022. (Keyword) レンサ球菌 / コレステロール依存性細胞溶解毒素 / 病原性
13.	SHIMIZU Tohya, Toshifumi Tomoyasu, TADA Yuya, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が保有する細胞壁アンカー型エンド-β-N-アセチルグルコサミニダーゼの機能解析, 第52回レンサ球菌研究会, Jul. 2022. (Keyword) レンサ球菌 / 糖鎖 / エンド-β-N-アセチルグルコサミニダーゼ
14.	Atsushi Tabata, YOKOHATA Shuto, Toshifumi Tomoyasu and Hideaki Nagamune : レンサ球菌が産生するペプチド溶血毒素ストレプトリジンSに対するTHP-1の応答反応, 第63回日本生化学会中国四国支部例会, May 2022. (Keyword) レンサ球菌 / 溶血毒素 / 病原性
15.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Functional analysis of a novel cell wall-anchored glycosidase of Streptococcus intermedius, 第95回細菌学会総会, Mar. 2022. (Keyword) Streptococci / グリコシダーゼ / 糖タンパク質 / 糖鎖
16.	ODA Hiroki, Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : Production and molecular characterization of mitilectin homolog derived from S. mitis, 第95回細菌学会総会, Mar. 2022. (Keyword) Streptococci / cytolysin / 宿主細胞定着因子
17.	YOKOHATA Shuto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Characterization of β-hemolysin produced by Streptococcus phocae, 第95回細菌学会総会, Mar. 2022. (Keyword) Streptococci / cytolysin / ストレプトリジンS / 細胞障害性
18.	KUBO Momoka, Atsushi Tabata, IKEDA Takuya, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : Response of human macrophage-like cells to pore-forming toxin produced by S. mitis clinical isolate, 第95回細菌学会総会, Mar. 2022. (Keyword) Streptococci / 川崎病 / cytolysin / inflammatory cytokine
19.	YOKOHATA Shuto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus phocae が産生するβ溶血因子の作用特性と病原性への寄与, 第74回⽇本細菌学会中国・四国⽀部総会, Oct. 2021. (Keyword) Streptococci / cytolysin / ストレプトリジンS / コレステロール依存性細胞溶解毒素
20.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Genetic analysis of the type VII secretion system of Streptococcus intermedius, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / Type VII輸送装置 / 病原性
21.	MIKI Haruka, Atsushi Tabata, 菊池賢, LIU HANYU, Toshifumi Tomoyasu and Hideaki Nagamune : Investigation on the cytotoxicity of a cholesterol-dependent cytolysin derived from Gemella bergeri, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / cytolysin / 細胞障害性
22.	Atsushi Tabata, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : Potential pathogenicity of S. mitis strain Nm-65 based on the complete genomic information, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / virulence factor / ゲノム情報
23.	ICHIJOH Ayu, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Purification of cell wall-anchored proteins of Streptococcus intermedius, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / extracellular matrix / 細胞壁アンカータンパク質
24.	IKEDA Takuya, Atsushi Tabata, Toshifumi Tomoyasu, 高尾亜由子, Hisashi Ohkuni and Hideaki Nagamune : Dual host cell-binding characteristics of the 5-domain-type CDC with N-terminal extra-domain derived from S. mitis, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / cytolysin / N末追加ドメイン
25.	SHIRAI Rina, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Investigation of the cellular response in THP-1 against Streptolysin S produced by S. anginosus, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / cytolysin / 免疫担当細胞
26.	Airi Matsumoto, Atsushi Tabata, Kazuto Ohkura, Chihiro Kodama, Hisashi Ohkuni, 高尾亞由子, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : Molecular characteristics of an adhesion molecule containing cholesterol-dependent cytolysin-motif produced by Mitis group streptococci, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / 細胞接着分子
27.	Airi Matsumoto, Atsushi Tabata, 高尾亜由子, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : ミチス群レンサ球菌が産生するコレステロール依存性細胞溶解毒素様の細胞接着分子の特性, 第73回日本細菌学会中国・四国支部総会, Oct. 2020.
28.	Airi Matsumoto, Atsushi Tabata, Kazuto Ohkura, Chihiro Kodama, Hisashi Ohkuni, 高尾亞由子, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : ミチス群レンサ球菌が産生するコレステロール依存性細胞溶解毒素モチーフを持つ細胞接着分子の特性, 第15回細菌学若手コロッセウム, Aug. 2020. (Keyword) レンサ球菌 / 細胞接着分子
29.	Atsushi Tabata, Kazuto Ohkura, Hisashi Ohkuni, Miho Kobayashi, Airi Matsumoto, Toshifumi Tomoyasu and Hideaki Nagamune : The structural and functional diversity of cholesterol-dependent cytolysin produced from Streptococci, 第20回日本蛋白質科学会年会, Jul. 2020.
30.	Airi Matsumoto, Atsushi Tabata, 高尾亞由子, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : Cholesterol-dependent cytolysin-like adhesion protein of Mitis group streptococci, 第20回日本蛋白質科学会年会, Jul. 2020.
31.	Toshifumi Tomoyasu, Mari Deguchi, Atsushi Tabata, 髙尾亞由子, 前田伸子 and Hideaki Nagamune : Streptococcus intermediusのヒアルロニダーゼ発現制御機構についての解析, 第93回日本細菌学会総会, Feb. 2020. (Keyword) ヒアルロニダーゼ / gene expression / Streptococci
32.	Airi Matsumoto, Atsushi Tabata, 髙尾亞由子, 菊池賢, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : ミチス群レンサ球菌が産生するコレステロール依存性細胞溶解毒素様の細胞接着分子, 第93回日本細菌学会総会, Feb. 2020. (Keyword) 細胞接着因子 / Streptococci / cytolysin
33.	Chihiro Kodama, Atsushi Tabata, Toshifumi Tomoyasu, 髙尾亞由子, 前田伸子 and Hideaki Nagamune : S. infantisが産生するコレステロール依存性細胞溶解毒素infantilysinの特性解析, 第93回日本細菌学会総会, Feb. 2020. (Keyword) cytolysin / cholesterol / Streptococci
34.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. pseudopneumoniaeが産生するコレステロール依存性細胞溶解毒素様の細胞接着分子, 第92回日本生化学会大会, Sep. 2019. (Keyword) 細胞接着 / レンサ球菌 / virulence factor
35.	Toshifumi Tomoyasu, Akiko Tominaga, Mari Deguchi, Eri Arimoto, Atsushi Tabata, 高尾亞由子, 前田伸子 and Hideaki Nagamune : Streptococcus intermedius が分泌する病原因子の特性解析, 第66回トキシンシンポジウム, Sep. 2019. (Keyword) cytolysin / ヒアルロニダーゼ / レンサ球菌
36.	Chihiro Kodama, QING TANG, Atsushi Tabata, 髙尾亞由子, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus infantisが産生する新規コレステロール依存性細胞溶解毒素infantilysinの作用特性の解明, 第13回細菌学若手コロッセウム, Aug. 2019. (Keyword) Streptococci / cytolysin
37.	Ayu Ichijoh, Toshifumi Tomoyasu, Eri Arimoto, Mari Deguchi, Atsushi Tabata, 高尾亞由子, 前田伸子 and Hideaki Nagamune : Streptococcus intermediusのヒアルロニダーゼ発現制御機構の解析, 第13回細菌学若手コロッセウム, Aug. 2019. (Keyword) 連鎖球菌 / ヒアルロン酸分解酵素 / extracellular matrix
38.	Rina Shirai, Miho Kobayashi, Atsushi Tabata, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitisが産生する非典型CDCに対する細胞の応答反応, 第13回細菌学若手コロッセウム, Aug. 2019. (Keyword) Streptococci / cytolysin
39.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus pseudopneumoniaeが産生するコレステロール依存性細胞溶解毒素様の細胞接着分子, 第13回細菌学若手コロッセウム, Aug. 2019. (Keyword) Streptococci / 細胞接着分子 / cytolysin
40.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus pseudopneumoniaeが産生するコレステロール依存性細胞溶解毒素様の細胞接着分子, 第51回レンサ球菌研究会, Jun. 2019. (Keyword) Streptococcus / cytolysin / 細胞接着分子
41.	Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosus subsp. anginosus由来溶原性ファージの遺伝子的特性, 第51回レンサ球菌研究会, Jun. 2019. (Keyword) Streptococcus / bacteriophage
42.	Toshifumi Tomoyasu, Mari Deguchi, 高尾亞由子, Atsushi Tabata, 前田伸子 and Hideaki Nagamune : Streptococcus intermediusが保有する分泌型グリコシダーゼの局在性, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / グリコシダーゼ / 局在性
43.	Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosus由来溶原性ファージの特性, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / bacteriophage
44.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. pseudopneumoniaeが産生するコレステロール依存性細胞溶解毒素様分子の特性解析, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / cytolysin / evolution
45.	Chihiro Kodama, QING TANG, Atsushi Tabata, 高尾亞由子, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus infantisが産生するinfantilysinの分子特性, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / cytolysin
46.	Miho Kobayashi, Atsushi Tabata, Hisashi Ohkuni, 高尾亞由子, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitisが産生する5ドメイン型CDCに対するヒト好中球様細胞の応答反応, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / cytolysin
47.	Yurina Nishihira, Atsushi Tabata, Toshifumi Tomoyasu, Kazuto Ohkura and Hideaki Nagamune : 薬剤キャリアのミセルが示す癌細胞障害性, 第22回バイオ治療法研究会学術集会, Dec. 2018. (Keyword) drug delivery system / cancer therapy
48.	Mari Deguchi, Toshifumi Tomoyasu, 高尾亞由子, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが保有するグリコシダーゼの局在性についての解析, 第71回日本細菌学会中国・四国支部総会, Oct. 2018. (Keyword) Streptococcus / グリコシダーゼ / 局在性
49.	山田拓矢, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Response of host human cells against SLS-homolog derived from S. anginosus subsp. anginosus, 第91回日本生化学会大会, Sep. 2018.
50.	児玉千紘, 唐卿, Atsushi Tabata, 髙尾亞由子, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus infantisが産生するInfantilysinの作用特性を明らかにする, 第12回細菌学若手コロッセウム in OKAYAMA, Aug. 2018.
51.	藤本あい, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitisが産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性の多様性に関する研究, 第12回細菌学若手コロッセウム in OKAYAMA, Aug. 2018.
52.	松本愛理, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus pseudopneumoniaeが保有するコレステロール依存性細胞溶解毒素様分子の解析, 第12回細菌学若手コロッセウム in OKAYAMA, Aug. 2018.
53.	Atsushi Tabata, 松本愛理, 藤本あい, 児玉千紘, Toshifumi Tomoyasu and Hideaki Nagamune : 咽頭口腔レンサ球菌が産生する溶血毒素とその多様性, 第12回細菌学若手コロッセウム in OKAYAMA, Aug. 2018.
54.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. pseudopneumoniaeが保有するコレステロール依存性細胞溶解毒素様分子の解析, 第65回トキシンシンポジウム, Jul. 2018. (Keyword) Streptococcus / cytolysin
55.	Ai Fujimoto, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitisが産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性, 第65回トキシンシンポジウム, Jul. 2018. (Keyword) Streptococcus / cytolysin / cholesterol
56.	Akiko Tominaga, Toshifumi Tomoyasu, Tatsuma Kusaka, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子 and Hideaki Nagamune : グループ3に属するコレステロール依存性細胞溶解毒素のCD59認識性の比較, 第65回トキシンシンポジウム, Jul. 2018. (Keyword) Streptococcus / cytolysin / cholesterol
57.	Atsushi Tabata, Seiya Otsuka, Deutsch Douglas, 菊池賢, Fischetti A. Vincent, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosus subsp. anginosusが保有するプラスミドとその特徴, 第50回レンサ球菌研究会, Jun. 2018. (Keyword) Streptococcus / プラスミド
58.	Toshifumi Tomoyasu, Masaki Matoba, Shingo Kusaka, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusのグリコシダーゼとインターメディリシン産生との関連について, 第50回レンサ球菌研究会, Jun. 2018. (Keyword) Streptococcus / virulence factor / cytolysin / sugar
59.	Haruka Hino, Tatsuya Okahata, Atsushi Tabata, 髙尾亞由子, 大國寿士, 小椋義俊, Toshifumi Tomoyasu, 林哲也, 前田伸子 and Hideaki Nagamune : Streptococcus mitisにおけるコレステロール依存性細胞溶解毒素の遺伝子分布パターンと細胞障害性との関連性, 第91回日本細菌学会総会, Mar. 2018.
60.	Risako Araki, Atsushi Tabata, 村上漱, 髙尾亞由子, Hisashi Ohkuni, 小椋義俊, Toshifumi Tomoyasu, 林哲也, 前田伸子 and Hideaki Nagamune : タンデム型末追加ドメインを持つコレステロール依存性細胞溶解毒素の特性解析, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
61.	Takuya Yamada, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Transcriptional response of host cells induced by SLS-producing S. anginosus subsp. anginosus, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
62.	高尾亞由子, Toshifumi Tomoyasu, Atsushi Tabata, Hideaki Nagamune and 前田伸子 : グリコシダーゼ活性が Streptococcus intermedius の実験的バイオフィルム量に及ぼす影響, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
63.	Yayoi Iwasa, Asuka Fukutomi, Atsushi Tabata, 村上漱, Toshifumi Tomoyasu and Hideaki Nagamune : Multiplex-PCR による高病原性 S. mitis 検出系の実用化に向けた検討, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
64.	Atsushi Tabata, Seiya Otsuka, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : S. anginosus subsp. anginosusにおけるプラスミドの保有状況とそれらの特性, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / virulence factor
65.	Toshifumi Tomoyasu, Akiko Tominaga, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子 and Hideaki Nagamune : DTT処理赤血球を用いたコレステロール依存性細胞溶解毒素の CD59認識性の比較, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
66.	Ai Fujimoto, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子, Toshifumi Tomoyasu and Hideaki Nagamune : S. mitis由来の新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性の多様性に関する研究, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
67.	Akiko Tominaga, Toshifumi Tomoyasu, Tatsuma Kusaka, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子 and Hideaki Nagamune : グループ3に属するコレステロール依存性細胞溶解毒素のCD59認識性の比較, 2017年度生命科学系学会合同年次大会, Dec. 2017. (Keyword) pathogenic microorganism / bacterial toxins
68.	Shingo Kusaka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : シアリダーゼ阻害剤がStreptococcus intermediusのシアリダーゼ活性や溶血活性に及ぼす効果, 2017年度生命科学系学会合同年次大会, Dec. 2017. (Keyword) pathogenic microorganism / virulence factor
69.	Kazuki Hatta, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ナノ粒子表面加工システムの構築に用いる細菌由来ペプチド転移酵素Sortase A組換え体の作製とその特性, 2017年度生命科学系学会合同年次大会, Dec. 2017. (Keyword) cancer therapy
70.	Chiho Okada, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : DDS用エフェクター分子としての細菌毒素組換え体の効率的な調製システムの構築, 2017年度生命科学系学会合同年次大会, Dec. 2017. (Keyword) cancer therapy
71.	Qing Tang, Masayoshi Onitsuka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 癌治療用新規DDSツール作製に用いるリガンド分子の調製とその機能評価, 第21回バイオ治療法研究会, Dec. 2017. (Keyword) cancer therapy
72.	Ai Fujimoto, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitis由来新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性を規定する構造領域の探索, 第70回日本細菌学会中国・四国支部総会, Oct. 2017. (Keyword) pathogenic microorganism / bacterial toxins
73.	Toshifumi Tomoyasu, Shingo Kusaka, Shinya Chiba, Takahiro Yamasaki, Atsushi Tabata and Hideaki Nagamune : ヒト血漿によるStreptococcus intermediusの病原性発現抑制機構の解析, 第70回日本細菌学会中国・四国支部総会, Oct. 2017. (Keyword) pathogenic microorganism / virulence factor
74.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. mitis由来5ドメイン型コレステロール依存性細胞溶解毒素のN末追加ドメインが示す細胞障害作用, 第11回細菌学若手コロッセウム, Aug. 2017. (Keyword) pathogenic microorganism / bacterial toxins
75.	Ai Fujimoto, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitis が産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性の多様性に関する研究, 第11回細菌学若手コロッセウム, Aug. 2017. (Keyword) pathogenic microorganism / bacterial toxins
76.	Toshifumi Tomoyasu, Atsushi Tabata, Shinya Chiba, Takahiro Yamasaki, Nozomi Takeda, Masaaki Tamaoka, Kazuto Ohkura and Hideaki Nagamune : 糖によるStreptococcus intermediusの病原性制御機構, 第64回トキシンシンポジウム, Jul. 2017. (Keyword) pathogenic microorganism / virulence factor
77.	Tatsuya Okahata, Atsushi Tabata, 小椋義俊, 林哲也, 高尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitis におけるコレステロール依存性細胞溶解毒素遺伝子の周辺遺伝子配座の多様性とその特徴, 第58回日本生化学会中国・四国支部例会, May 2017. (Keyword) bacterial toxins / gene
78.	Seiya Ohtsuka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosus subsp. anginosusが保有する新規Extra-chromosomal DNAの分子特性, 第90回日本細菌学会総会, Mar. 2017. (Keyword) Streptococcus / プラスミド / 可動遺伝子
79.	Masaki Matoba, Toshifumi Tomoyasu, Ayuko Takao, Atsushi Tabata, nobuko Maeda and Hideaki Nagamune : Streptococcus intermediusの高病原性株スクリーニングシステムの開発, 第90回日本細菌学会総会, Mar. 2017. (Keyword) Streptococcus / virulence factor / cytolysin
80.	Tatsuya Okahata, Syu Murakami, Atsushi Tabata, Yoshitoshi Ogura, Tetsuya Hayashi, Ayuko Takao, Hisashi Ohkuni, Toshifumi Tomoyasu, Nobuko Maeda and Hideaki Nagamune : Streptococcus mitisが保有するコレステロール依存性細胞溶解毒素遺伝子周辺における遺伝子配座の多様性, 第90回日本細菌学会総会, Mar. 2017. (Keyword) Streptococcus / cytolysin / genome
81.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. mitis由来5ドメイン型コレステロール依存性細胞溶解毒素のN末追加ドメインが示す細胞障害作用, 第90回日本細菌学会総会, Mar. 2017. (Keyword) Streptococcus / cytolysin
82.	Tatsuma Kusaka, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : ウマ赤血球に存在するExD-CDCレセプターの探索, 第3回日本生物工学会西日本支部講演会, Dec. 2016. (Keyword) Streptococcus / cytolysin / CD59
83.	Ai Fujimoto, Atsushi Tabata, Ayuko Takao, Hisashi Ohkuni, Nobuko Maeda, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitisが産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性の多様性, 第3回日本生物工学会西日本支部講演会, Dec. 2016. (Keyword) Streptococcus / cytolysin
84.	Takuya Saigoh, Atsushi Tabata, Ayuko Takao, Hisashi Ohkuni, Nobuko Maeda, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitisにおける効果的な形質転換法の検討, 第3回日本生物工学会西日本支部講演会, Dec. 2016. (Keyword) Streptococcus / 形質転換法 / プラスミド / DNA断片
85.	Atsushi Tabata, Kazuto Ohkura, Youhei Tatematsu, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な細胞障害性を示す細菌毒素に対する糖の阻害作用, 第20回バイオ治療法研究会, Dec. 2016. (Keyword) Streptococcus / cytolysin / sugar
86.	Shingo Kusaka, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が産生するシアリダーゼの発現制御機構の解析, 第69回日本細菌学会中国・四国支部総会, Oct. 2016. (Keyword) Streptococcus / cytolysin / sugar
87.	Ikumi Tamura, Atsushi Tabata, Syu Murakami, Ayuko Takao, Toshifumi Tomoyasu, Nobuko Maeda and Hideaki Nagamune : Streptococcus infantis が産生する新規コレステロール依存性細胞溶解毒素Infantilysin, 第63回トキシンシンポジウム, Jul. 2016. (Keyword) Streptococcus / cytolysin
88.	Toshifumi Tomoyasu, Shinya Chiba, Takahiro Yamasaki, Shingo Kusaka, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius の血液成分による病原性亢進とヒト血液成分によるその防御, 第48回レンサ球菌研究会, Jul. 2016. (Keyword) Streptococcus / cytolysin / sugar / antibody
89.	Ayuko Takao, Hideaki Nagamune, Toshifumi Tomoyasu and Nobuko Maeda : Effects of quorum sensing peptides and environmental factors on Streptococcus intermedius, 第89回日本細菌学会総会, Mar. 2016. (Keyword) Streptococcus / quorum sensing / cytolysin
90.	Ikumi Tamura, Atsushi Tabata, Shu Murakami, Ayuko Takao, Hisashi Ohkuni, Toshifumi Tomoyasu, Nobuko Maeda and Hideaki Nagamune : Cytotoxic properties of a novel cholesterol-dependent cytolysin from Streptococcus infantis, 第89回日本細菌学会総会, Mar. 2016. (Keyword) Streptococcus / cytolysin / function
91.	Hiromi Ohtani, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptolysin S homolog-dependent cytotoxicity of betahemolytic S. anginosus subsp. anginosus, 第89回日本細菌学会総会, Mar. 2016. (Keyword) Streptococcus / cytolysin / function / gene expression
92.	Toshifumi Tomoyasu, Shinya Kusaka, Masaki Matoba, Yukihiro Kaneko, Atsushi Tabata and Hideaki Nagamune : Wide upstream region of ily is involved in its repression in Streptococcus intermedius, 第89回日本細菌学会総会, Mar. 2016. (Keyword) Streptococcus / cytolysin / gene expression
93.	Shinya Chiba, Toshifumi Tomoyasu, Takahiro Yamasaki, Shingo Kusaka, Atsushi Tabata and Hideaki Nagamune : Positive and negative control of ily expression by blood components, 第89回日本細菌学会総会, Mar. 2016. (Keyword) Streptococcus / cytolysin / blood / sugar
94.	Qing Tang, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : A trial for development of effective drug delivery system using small targeting module against CEA-positive cancer, Joint Meeting of the 38th Annual Meeting of the Molecular Biology Society of Japan and the 88th Annual Meeting of the Japanese Biochemical Society, Dec. 2015. (Keyword) drug delivery system / antibody
95.	Ryosuke Tanatsugu, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Functional analysis of a gram-negative characteristic segment of DnaK using Streptococcus intermedius DnaK, 第38回日本分子生物学会年会, Dec. 2015. (Keyword) Streptococcus / molecular chaperone / protein
96.	Shinya Kusaka, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Investigation of transcriptional regulation elements in ily promoter region of Streptococcus intermedius, 第38回日本分子生物学会年会, Dec. 2015. (Keyword) Streptococcus / cytolysin / gene expression
97.	Shinya Chiba, Toshifumi Tomoyasu, Takahiro Yamasaki, Atsushi Tabata and Hideaki Nagamune : 血液成分によるインターメディリシン発現調節機構の解析, 第68回日本細菌学会中国・四国支部総会, Oct. 2015. (Keyword) Streptococcus / cytolysin / sugar / blood
98.	Ikumi Tamura, Atsushi Tabata, Shu Murakami, Ayuko Takao, Hisashi Ohkuni, Toshifumi Tomoyasu, Nobuko Maeda and Hideaki Nagamune : Streptococcus infantis由来の新規コレステロール依存性細胞溶解毒素の作用特性, 第68回日本細菌学会中国・四国支部総会, Oct. 2015. (Keyword) Streptococcus / cytolysin / virulence factor
99.	Toshifumi Tomoyasu, Shinya Chiba, Takahiro Yamasaki, 甲斐瑛之, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusのグリコシダーゼによるインターメディリシン発現調節機構の解析, 第56回日本生化学会中国四国支部例会, May 2015. (Keyword) Streptococci / enzyme / sugar / cytolysin / gene expression
100.	Kentaro Maya, Atsushi Tabata, Kazuto Ohkura, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : S. anginosus subsp. whileyi およびS. constellatus subsp. viborgensis が保有するβ溶血因子の特性解析, 第88回日本細菌学会総会, Mar. 2015. (Keyword) Streptococci / cytolysin / function
101.	Atsushi Morishita, Atsushi Tabata, Shu Murakami, 高尾亞由子, Hisashi Ohkuni, 小椋義俊, 林哲也, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : S. mitis におけるコレステロール依存性細胞溶解毒素遺伝子の分布とβ-ラクタム系薬剤耐性の関連性, 第88回日本細菌学会総会, Mar. 2015. (Keyword) Streptococci / antibiotics / cytolysin
102.	Takahiro Yamasaki, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : S. intermedius が保有するグリコシダーゼがインターメディリシン発現制御に果たす役割についての解析, 第88回日本細菌学会総会, Mar. 2015. (Keyword) Streptococci / gene expression / enzyme / sugar
103.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が保有するシアリダーゼの精製とその性状の解析, 第88回日本細菌学会総会, Mar. 2015. (Keyword) Streptococci / protein / sugar
104.	Hajime Yoshida, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Inerolysin (INY) の pH 依存的な膜孔形成活性と立体構造変化, 第133回徳島生物学会総会, Dec. 2014. (Keyword) pathogenic microorganism / Streptococci / cytolysin / pH
105.	Yukimasa Okubo, Natsuki Anyohji, Atsushi Tabata, 北條恵子, Toshifumi Tomoyasu, 立松洋平, Kazuto Ohkura and Hideaki Nagamune : ドラッグデリバリーシステム創成を目指したSortase Aによるペプチド修飾化リポソーム作製技術の開発, 第18回バイオ治療法研究会, Dec. 2014. (Keyword) drug delivery system / Sortase A / liposomes
106.	Yukimasa Okubo, Natsuki Anyohji, Atsushi Tabata, 北條恵子, Toshifumi Tomoyasu and Hideaki Nagamune : 新規ドラッグデリバリーシステムツール作製法としてのペプチド修飾化リポソームの作製, 第87回日本生化学会大会, Oct. 2014. (Keyword) drug delivery system / liposomes / ガン治療
107.	Masaaki Tamaoka, Nozomi Takeda, Atsushi Tabata, Kazuto Ohkura, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の膜孔形成活性に対する糖の抑制効果, 第87回日本生化学会大会, Oct. 2014. (Keyword) pathogenic microorganism / Streptococcus / virulence factor / sugar / cytolysin
108.	Natsuki Anyohji, Atsushi Tabata, Yukimasa Okubo, Toshifumi Tomoyasu and Hideaki Nagamune : 細菌由来ペプチド転移酵素Sortase Aの由来菌種依存的な基質認識特性, 第87回日本生化学会大会, Oct. 2014. (Keyword) グラム陽性菌 / ブドウ球菌 / Streptococcus / Sortase A / 基質特異性
109.	Atsushi Morishita, Atsushi Tabata, Shu Murakami, 高尾亞由子, 勝部康弘, Hisashi Ohkuni, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitisにおける膜孔形成毒素遺伝子の保有とβ-ラクタム薬耐性の関連性, 第67回日本細菌学会中国四国支部総会, Oct. 2014. (Keyword) pathogenic microorganism / Streptococcus / virulence factor / 溶血因子 / 薬剤耐性
110.	Takahiro Yamasaki, Toshifumi Tomoyasu, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusの病原性とグリコシダーゼとの関連性, 第67回日本細菌学会中国四国支部総会, Oct. 2014. (Keyword) pathogenic microorganism / Streptococcus / sugar / グリコシダーゼ
111.	Toshifumi Tomoyasu, 今木英統, Chiharu Taue, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が保有するグリコシダーゼの病原性に果たす役割について, 第61 回トキシンシンポジウム ∼鳴門渦潮カンファレンス∼, Sep. 2014. (Keyword) Streptococcus / pathogenic microorganism / sugar / グリコシダーゼ
112.	Atsushi Tabata, Kentaro Maya, 大谷浩美, Yuji Sato, Kota Nakano, Kazuto Ohkura, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : β溶血性アンギノーサス群レンサ球菌が保有するストレプトリジンSホモログの多様性, 第46回レンサ球菌研究会, Jun. 2014. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / 溶血因子
113.	Atsushi Tabata, Nozomi Takeda, Masaaki Tamaoka, Toshifumi Tomoyasu, 高尾亞由子, 前田伸子, Hisashi Ohkuni and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の膜孔形成活性に及ぼす糖の影響, 第55回日本生化学会中国・四国支部例会, Jun. 2014. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / sugar
114.	Toshifumi Tomoyasu, 今木英統, Chiharu Taue, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが保有する多基質酵素``MsgA''の性状解析, 第55回日本生化学会中国・四国支部例会, Jun. 2014. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / 糖鎖 / グリコシダーゼ
115.	Toshifumi Tomoyasu, Yukihiro Kaneko, Atsushi Tabata and Hideaki Nagamune : Identification and study of the binding region of ily transcriptional repressive element, 第87回日本細菌学会総会, Mar. 2014. (Keyword) Streptococci / 転写抑制因子結合部位 / gene expression / cytolysin
116.	Shu Murakami, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : 高病原性Streptococcus mitisの検出・同定を目的とした新規検査システムの開発, 第87回日本細菌学会総会, Mar. 2014. (Keyword) Streptococci / identification / PCR / cytolysin
117.	Naoki Yamamoto, Toshifumi Tomoyasu, 今木英統, Atsushi Tabata and Hideaki Nagamune : Characterization of a novel secreted glycosidase (MsgA) of Streptococcus intermedius, 第87回日本細菌学会総会, Mar. 2014. (Keyword) Streptococci / グリコシダーゼ / 糖鎖 / decomposition
118.	Natsuki Anyohji, Atsushi Tabata, 大久保行将, Toshifumi Tomoyasu and Hideaki Nagamune : Comparison of the transition activity of Sortase A using GFP-substrate panel, 第87回日本細菌学会総会, Mar. 2014. (Keyword) enzyme / ペプチド転位酵素 / GFP
119.	金惠珍, Atsushi Tabata, Toshifumi Tomoyasu, 上野友美, 内山成人, Keizo Yuasa, Akihiko Tsuji and Hideaki Nagamune : エストロゲン作用物質が示す骨芽細胞分化促進作用の解析, 徳島生物学会, Dec. 2013. (Keyword) エストロゲン / 骨芽細胞分化
120.	Atsushi Tabata, 安養寺夏希, 大久保行将, Toshifumi Tomoyasu and Hideaki Nagamune : 細菌由来ペプチド転移酵素Sortase Aを用いたDDS用新規機能性リポソームの創成に関する検討, 第17回バイオ治療法研究会学術集会, Dec. 2013. (Keyword) bacteria / drug delivery system / liposomes / ペプチド転移酵素 / GFP
121.	Toshifumi Tomoyasu, Hidenori Imaki, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : Identification and characterization of MsgA, a novel secreted glycosidase of Streptococcus intermedius, 第36回日本分子生物学会年会, Dec. 2013. (Keyword) Streptococcus / pathogenic microorganism / sugar / enzyme
122.	Shu Murakami, Atsushi Tabata, 髙尾亞由子, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : 高病原性Streptococcus mitis検出・同定システムの構築, 第66回日本細菌学会中国・四国支部総会, Oct. 2013. (Keyword) Streptococcus / pathogenic microorganism / identification / PCR
123.	Naoki Yamamoto, Toshifumi Tomoyasu, 今木英統, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが分泌する新規グリコシダーゼの発見と性状解析, 第66回日本細菌学会中国・四国支部総会, Oct. 2013. (Keyword) Streptococcus / pathogenic microorganism / sugar / enzyme
124.	Natsuki Anyohji, Atsushi Tabata, Yukimasa Okubo, Toshifumi Tomoyasu and Hideaki Nagamune : 細菌由来ペプチド転移酵素Sortase Aの比較解析 -新規DDS開発への応用を目指して-, 日本生化学会, Sep. 2013. (Keyword) bacteria / drug delivery system / 蛍光タンパク質 / ペプチド転移酵素
125.	Nozomi Takeda, Atsushi Tabata, Asuka Nogami, 髙尾亞由子, Hisashi Ohkuni, 前田伸子, Toshifumi Tomoyasu and Hideaki Nagamune : N末に追加ドメインを有するコレステロール依存性細胞溶解毒素の作用特性, 日本生化学会, Sep. 2013. (Keyword) cytolysin / protein / cholesterol / sugar
126.	Atsushi Tabata, Kazuto Ohkura, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の受容体認識および作用特性における多様性, 第60回毒素シンポジウム, Jul. 2013. (Keyword) Streptococcus / pathogenic microorganism / gene expression / virulence factor
127.	Toshifumi Tomoyasu, Hidenori Imaki, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius の主要病原因子であるインターメディリシンの発現調節機構の解析, 第60回毒素シンポジウム, Jul. 2013. (Keyword) Streptococcus / pathogenic microorganism / gene expression / virulence factor
128.	Atsushi Tabata, 中野晃太, Kazuto Ohkura, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : β溶血性 Streptococcus anginosus が保有するストレプトリジンS ホモログの特徴と細胞障害性への寄与, 第22回 Lancefieldレンサ球菌研究会, Jun. 2013. (Keyword) Streptococcus / pathogenic microorganism / virulence factor
129.	Hidenori Imaki, Toshifumi Tomoyasu, 増田早智子, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : 糖タンパク質によるStreptococcus intermediusのily発現促進機構の解析, 第22回 Lancefieldレンサ球菌研究会, Jun. 2013. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / gene expression
130.	Toshifumi Tomoyasu, Hiroyuki Kondo, Masanori Oisugi, Atsushi Tabata and Hideaki Nagamune : グラム陽性菌と陰性菌のDnaKシャペロンシステムの比較, 第54回日本生化学会中国・四国支部例会, Jun. 2013. (Keyword) DnaK / ClpB / Gram-Positive Bacteria / Gram-Negative Bacteria / molecular chaperone
131.	Asuka Nogami, Atsushi Tabata, Nozomi Takeda, Ayuko Takao, Hisashi Ohkuni, Nobuko Maeda, Toshifumi Tomoyasu and Hideaki Nagamune : β溶血性の高病原性Streptococcus mitisサブグループの特性, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / clinical laboratory testing
132.	Yukihiro Kaneko, Toshifumi Tomoyasu, Hidenoro Imaki, Atsushi Tabata and Hideaki Nagamune : ily転写抑制因子の結合領域の探索, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / gene expression
133.	Atsushi Tabata, Yuji Sato, Kota Nakano, Kazuto Ohkura, Ken Kikuti, Toshifumi Tomoyasu and Hideaki Nagamune : S. constellatus subsp. constellatusが保有するβ溶血因子の探索, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / enzyme
134.	Nozomi Takeda, Atsushi Tabata, Asuka Nogami, Ayuko Takao, Hisashi Ohkuni, Nobuko Maeda, Toshifumi Tomoyasu and Hideaki Nagamune : 新規5ドメイン型コレステロール依存性細胞溶解毒素の分子特性, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / enzyme
135.	Miku Ishikawa, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な膜孔形成毒素インターメディリシンにより好中球に誘導される応答反応, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / 細胞感染
136.	Hidenori Imaki, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Identification of an expressionpromoting factor for ily of Streptococcus intermedius, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / gene expression
137.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Does DnaK from Gram-positive Bacterium recognize ClpB of E.coli?, 第86回日本細菌学会総会, Mar. 2013. (Keyword) molecular chaperone / Streptococcus / enzyme
138.	Kenji Nagataki, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Investigation on the procedure for enhancement of cellulase activity and its application, 日本生化学会, Dec. 2012. (Keyword) molecular chaperone / セルラーゼ / バイオエタノール / application
139.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Small heat shock protein AgsA is an effective stabilizer of enzyme activities, 日本生化学会, Dec. 2012. (Keyword) molecular chaperone / sHSP / enzyme
140.	Hyejin Kim, Atsushi Tabata, Toshifumi Tomoyasu, Tomomi Ueno, Naruhito Uchiyama, Keizo Yuasa, Akihiko Tsuji and Hideaki Nagamune : A study on the mechanism of osteoblast differentiation induced by estrogen-stimuli, 日本生化学会, Dec. 2012. (Keyword) osteoblast / エストロゲン / イソフラボン
141.	Manami Aoyagi, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : インターメディリシンの細胞膜結合能と分子集合メカニズムの解析, 徳島生物学会, Dec. 2012. (Keyword) Streptococci / cytolysin / 細胞膜
142.	Yasunori Iwano, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : インターメディリシン刺激が単球系細胞THP-1の遺伝子発現に及ぼす影響, 徳島生物学会, Dec. 2012. (Keyword) Streptococci / cytolysin / gene expression
143.	Masanori Oisugi, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : 大腸菌のClpBは連鎖球菌のDnaKシャペロンシステムを認識するのか, 徳島生物学会, Dec. 2012. (Keyword) molecular chaperone / Hsp70 / Hsp104 / DnaK / ClpB
144.	Nozomi Takeda, Atsushi Tabata, Ayuko Takao, Hisashi Ohkuni, Toshifumi Tomoyasu and Atsushi Tabata : Streptococcus mitis が産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性, 日本細菌学会, Oct. 2012. (Keyword) Streptococci / Streptococcus mitis / コレステロール依存性細胞溶解毒素
145.	Yukihiro Kaneko, Toshifumi Tomoyasu, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : ily 発現抑制因子が認識するコンセンサス配列の探索, 日本細菌学会, Oct. 2012. (Keyword) Streptococci / gene expression / コンセンサス配列
146.	Atsushi Tabata, 中野晃太, Kazuto Ohkura, Toshifumi Tomoyasu and 菊池賢 : アンギノーサス群連鎖球菌が保有するβ溶血因子の探索とその特性, 第59回毒素シンポジウム, Aug. 2012.
147.	Atsushi Tabata, 中野晃太, 大倉一人, Toshifumi Tomoyasu, 菊池賢 and Hideaki Nagamune : β溶血性Streptococcus anginosusが保有するペプチド性溶血因子の分子特性, 第6回細菌学若手コロッセウム, Aug. 2012.
148.	金惠珍, Atsushi Tabata, Toshifumi Tomoyasu, 上野友美, 内山成人 and Hideaki Nagamune : Effect of Equol, an Enterobacterial Metabolite of Soybean Isoflavones on Osteoblast Differentiation., 第16回腸内細菌学会, Jun. 2012.
149.	今木英統, Toshifumi Tomoyasu, 増田早智子, Atsushi Tabata and Hideaki Nagamune : LacRはStreptococcus intermediusのily発現の主要な制御因子である, 第21回 Lancefieldレンサ球菌研究会, Jun. 2012.
150.	Atsushi Tabata, 野上明日香, 竹田望, 髙尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : コレステロール依存性細胞溶解毒素遺伝子を保有するStreptococcus mitis株の毒素産生特性とヒト細胞障害性, 第21回 Lancefieldレンサ球菌研究会, Jun. 2012.
151.	金惠珍, Atsushi Tabata, Toshifumi Tomoyasu, 上野友美, 内山成人, Keizo Yuasa, Akihiko Tsuji and Hideaki Nagamune : エストロゲン作用物質が示す骨芽細胞の分化促進作用, 第53回日本生化学会中国・四国支部例会, May 2012.
152.	Toshifumi Tomoyasu, 今木英統, Atsushi Tabata and Hideaki Nagamune : グラム陽性菌と陰性菌のコシャペロンによるDnaK活性化機構の比較, 第85回日本細菌学会総会, Mar. 2012. (Keyword) Streptococci / molecular chaperone / protein
153.	今木英統, Toshifumi Tomoyasu, 増田早智子, Atsushi Tabata and Hideaki Nagamune : ILYを高産生するStreptococcus intermediusの臨床分離株の多くがLacRに変異を持つ, 第85回日本細菌学会総会, Mar. 2012. (Keyword) Streptococci / cytolysin / gene expression
154.	Atsushi Tabata, 中野晃太, Toshifumi Tomoyasu, 大倉一人, 菊池賢 and Hideaki Nagamune : TOMM family peptides decide the hemolytic character of Streptococcus anginosus, 第85回日本細菌学会総会, Mar. 2012. (Keyword) Streptococci / bacterial toxins
155.	宮崎彩, 鶴野圭悟, Toshifumi Tomoyasu and 園元謙二 : Streptococcus intermedius DnaK システムのin vitroにおける機能解析, 第18回日本生物工学会九州支部福岡大会, Dec. 2011. (Keyword) Streptococci / molecular chaperone / protein
156.	福居孝之, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の膜孔形成反応における分子動態の解析, 第127回徳島生物学会, Dec. 2011. (Keyword) Streptococci / cytolysin
157.	Atsushi Tabata, 大久保行将, Toshifumi Tomoyasu and Hideaki Nagamune : 膜孔形成性キメラ毒素の新規DDSツールとしての応用性に関する検討, 第15回バイオ治療法研究会学術集会, Dec. 2011. (Keyword) cancer therapy
158.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが保有するDnaKシャペロンシステムの機能解析, 第64回日本細菌学会中国・四国支部総会, Oct. 2011. (Keyword) Streptococci / molecular chaperone
159.	中野晃太, Atsushi Tabata, Toshifumi Tomoyasu, 大倉一人, 菊池賢, 平松啓一 and Hideaki Nagamune : β溶血性Streptococcus anginosusで見出された新規ペプチド性溶血因子, 第64回日本細菌学会中国・四国支部総会, Oct. 2011. (Keyword) Streptococci / bacterial toxins
160.	今木英統, Toshifumi Tomoyasu, 増田早智子, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusのily発現調節因子の探索, 第64回日本細菌学会中国・四国支部総会, Oct. 2011. (Keyword) Streptococci / cytolysin / gene expression
161.	大久保行将, Atsushi Tabata, 田村仁人, Toshifumi Tomoyasu and Hideaki Nagamune : 細胞標的化キメラ細菌毒素を用いた新規DDSツールの開発, 第84回日本生化学会大会, Sep. 2011. (Keyword) cancer therapy
162.	岡久奈緒美, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : キノコβ-グルカンによるマクロファージ様THP-1の活性化作用, 第84回日本生化学会大会, Sep. 2011. (Keyword) cancer immunotherapy
163.	Atsushi Tabata, 中野晃太, Toshifumi Tomoyasu and Hideaki Nagamune : アンギノーサス群連鎖球菌が保有する溶血因子に関する検討, 第5回細菌学若手コロッセウム, Aug. 2011. (Keyword) Streptococci / bacterial toxins
164.	Toshifumi Tomoyasu, 今木英統, 増田早智子, Atsushi Tabata and Hideaki Nagamune : コレステロール依存性細胞溶解毒素intermedilysinの発現調節因子がStreptococcus intermediusの病原性に果たす役割の解析, 第58回トキシンシンポジウム, Jul. 2011. (Keyword) Streptococci / cytolysin
165.	Atsushi Tabata, 中野晃太, Toshifumi Tomoyasu and Hideaki Nagamune : アンギノーサス群連鎖球菌が保有する溶血因子の探索, 第20回Lancefieldレンサ球菌研究会/第43回レンサ球菌感染症研究会, Jun. 2011.
166.	Toshifumi Tomoyasu, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : カタボライト抑制因子CcpAによるStreptococcus intermediusのヒト特異的細胞溶解毒素intermedilysinの発現調節, 第33回日本分子生物学会年会第83回日本生化学会大会合同大会, Dec. 2010.
167.	Atsushi Tabata, 山本泰裕, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : 2種のコレステロール依存性細胞溶解毒素を産生するStreptococcus mitis Nm-65株の細胞障害性に関する検討, 第33回日本分子生物学会年会第83回日本生化学会大会合同大会, Dec. 2010.
168.	田村仁人, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 細菌由来タンパク質をベースとしたDDSツールの開発-標的細胞に対する選択的送達能に関する検討-, 第125回徳島生物学会, Dec. 2010.
169.	村田貴洋, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : コレステロール依存性細胞溶解毒素による宿主細胞の応答反応の検討, 第125回徳島生物学会, Dec. 2010.
170.	Atsushi Tabata, Kota Nakano, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosusが保有する細胞傷害因子に関する検討, 第63回日本細菌学会中国・四国支部総会, Oct. 2010.
171.	増田早智子, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : 血液成分によるily遺伝子の発現調節, 第63回日本細菌学会中国・四国支部総会, Oct. 2010.
172.	山本泰裕, Atsushi Tabata, Toshifumi Tomoyasu, Katsuhiko Hirota, 大国寿士 and Hideaki Nagamune : 川崎病患児由来Streptococcus mitis Nm-65株が産生する2種類のコレステロール依存性細胞溶解毒素遺伝子の発現とその病原性への寄与, 第57回トキシンシンポジウム, Jul. 2010.
173.	Atsushi Tabata, 鈴木圭祐, Toshifumi Tomoyasu and Hideaki Nagamune : 細胞膜構造に依存したインターメディリシンの作用特性, 第51回日本生化学会中国・四国支部例会, May 2010.
174.	今木英統, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius ccpA破壊株とcre変異株の細胞毒性の解析, 第83回日本細菌学会総会, Mar. 2010. (Keyword) virulence factor
175.	Toshifumi Tomoyasu, 今木英統, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius dnaK破壊相補株の表現型の解析, 第83回日本細菌学会総会, Mar. 2010. (Keyword) virulence factor
176.	山本泰裕, Atsushi Tabata, Toshifumi Tomoyasu, Katsuhiko Hirota, Yoichiro Miyake, Hideaki Nagamune and 大國寿士 : Analysis of a novel S.mitis strain possessing two distinct cholesterol-dependent cytolysin genes, 第83回日本細菌学会総会, Mar. 2010.
177.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Dissection of the chaperone function of the small heat shock protein AgsA, 第32回日本分子生物学会年会, Dec. 2009.
178.	Atsushi Tabata, 金惠珍, Toshifumi Tomoyasu, Hiroki Kourai, 澤田千恵子, 下野生世, Motoyuki Sugai, 赤松優 and Hideaki Nagamune : 融合PCRイムノクロマトグラフィーによる迅速微生物検査系の構築, 日本防菌防黴学会 2009年度若手の会, Dec. 2009.
179.	Atsushi Tabata, 三好宗一郎, 天河崇, Toshifumi Tomoyasu and Hideaki Nagamune : 脂質ラフトを反応場とするStreptococcus intermediusのヒト細胞感染機構, 第82回日本生化学会大会, Oct. 2009.
180.	垣口貴沙, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的細胞溶解毒素の膜貫入領域が膜孔形成反応において果たす機能の解析, 第82回日本生化学会大会, Oct. 2009.
181.	鈴木圭祐, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 多様な受容体認識性を示すコレステロール依存性細胞溶解毒素の細胞膜構造に依存した作用特性, 第62回日本細菌学会中国・四国支部総会, Oct. 2009.
182.	伊藤貴洋, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 蛍光性Streptococcus intermedius株の作製, 第62回日本細菌学会中国・四国支部総会, Oct. 2009.
183.	Atsushi Tabata, Keisuke Suzuki, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : 標的細胞膜構造がコレステロール依存性細胞溶解毒素の受容体認識多様性に及ぼす影響, 若手研究者育成のためのワークショップ若手コロセウム(III), Oct. 2009.
184.	Toshifumi Tomoyasu, Atsushi Tabata, 菊池賢, 佐々木崇, 馬場理, 平松啓一 and Hideaki Nagamune : Streptococcus intermediusが産生するヒト特異的細胞溶解毒素インターメディリシンの発現調節機構の解析, 第56回トキシンシンポジウム, 106-109, Aug. 2009.
185.	Toshifumi Tomoyasu, 廣島理樹, 今木英統, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusのily発現調節機構の解析, 第18回 Lancefield レンサ球菌研究会, Jun. 2009.
186.	Atsushi Tabata, 篠原由樹, 鈴木圭祐, Toshifumi Tomoyasu and Hideaki Nagamune : インターメディリシンの膜孔形成に携わる分子構造と機能に関する解析, 第18回 Lancefieldレンサ球菌研究会, Jun. 2009.
187.	Atsushi Tabata, 篠原由樹, Toshifumi Tomoyasu and Hideaki Nagamune : インターメディリシンの分子間相互作用に寄与する部分構造の解析, 第50回日本生化学会中国・四国支部例会, May 2009.
188.	Toshifumi Tomoyasu, Atsushi Tabata, 菊池賢, 佐々木崇, 馬場理, 平松啓一 and Hideaki Nagamune : カタボライト抑制因子CcpAによるヒト特異的細胞溶解毒素インターメディリシンの発現調節機構の解析, 第82回日本細菌学会総会, Mar. 2009.
189.	垣口貴沙, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な細胞溶解毒素インターメディリシン(ILY)の膜孔形成を誘導する構造変化領域の解析, 第82回日本日本細菌学会総会, Mar. 2009.
190.	金惠珍, Toshifumi Tomoyasu, Atsushi Tabata, 菅井基行, 赤松優 and Hideaki Nagamune : 融合PCRイムノクロマトグラフィーによる迅速細菌検査, 第82回日本細菌学会総会, Mar. 2009.
191.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptooccus intermediusのストレス誘導型シャペロンDnaKの機能解析, 第82回日本日本細菌学会総会, Mar. 2009.
192.	齋藤静香, Atsushi Tabata, 坂倉永里子, 鈴木圭祐, 垣口貴沙, 篠原由樹, 福島江, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の受容体認識特性に関する検討, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, Dec. 2008.
193.	坂倉永里子, Atsushi Tabata, 齋藤静香, Toshifumi Tomoyasu and Hideaki Nagamune : 癌標的化毒素を用いた癌療法のための効果的DDSの開発, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, Dec. 2008.
194.	廣島理樹, Toshifumi Tomoyasu, 小南章, Atsushi Tabata, 菊池賢, 佐々木崇, 馬場理, 平松啓一 and Hideaki Nagamune : Streptococcus intermediusが保有するヒト特異的細胞溶解毒素インターメディリシンをコードするily遺伝子のプロモーター領域の解析, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, Dec. 2008.
195.	石川洋子, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : サルモネラ属細菌が保有する小型分子シャペロンAgsAのN末端とC末端領域の機能解析, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, Dec. 2008.
196.	垣口貴沙, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な細胞溶解毒素インターメディリシンの膜孔形成に関与する分子構造の解析, 第120回徳島生物学会, Nov. 2008.
197.	Atsushi Tabata, 齋藤静香, 坂倉永里子, 鈴木圭祐, 篠原由樹, 福島江, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : コレステロール及びヒト型CD59を受容体とするCholesterol-dependent cytolysin:Sm-hPAFのコレステロール認識特性に関する検討, 第61回日本細菌学会中国・四国支部総会, Oct. 2008.
198.	三好宗一郎, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus intermediusのヒト細胞感染現象におけるインターメディリシンと宿主細胞膜構造の役割, 第61回日本細菌学会中国・四国支部総会, Oct. 2008.
199.	Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 連鎖球菌属が産生するコレステロール依存性細胞溶解毒素の受容体認識における多様性, 第2回細菌学若手コロッセウム, Aug. 2008.
200.	廣島理樹, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : ヒト特異的細胞溶解毒素インターメディリシンの発現調節機構の解析, 第17回 Lancefieldレンサ球菌研究会, Jul. 2008.
201.	Atsushi Tabata, 齋藤静香, 坂倉永里子, 鈴木圭祐, 山本泰裕, 篠原由樹, 福島江, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : ヒトCD59指向性コレステロール依存性細胞溶解毒素の受容体認識特性に関する検討, 第17回 Lancefieldレンサ球菌研究会, Jul. 2008.
202.	石川洋子, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : サルモネラ属細菌が保有する小型分子シャペロンAgsAの機能解析, 第49回日本生化学会中国・四国支部例会, May 2008.
203.	垣口貴沙, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な細胞溶解毒素インターメディリシン(ILY)の膜孔形成に関わる部分構造に関する解析, 第49回日本生化学会中国・四国支部例会, May 2008.
204.	Atsushi Tabata, Souichirou Miyoshi, Toshifumi Tomoyasu and Hideaki Nagamune : 宿主細胞膜構造がStreptococcus intermediusのヒト細胞感染に及ぼす影響, 第81回日本細菌学会総会, Mar. 2008. (Keyword) Streptococcus / Lipid raft / infection
205.	Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : ヒト特異的な細胞溶解毒素インターメディリシンの発現調節の遺伝学的解析, 第81回日本細菌学会総会, Mar. 2008.
206.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : 連鎖球菌(S. intermedius)ClpP破壊株の作成とその表現型の解析, 第81回日本細菌学会総会, Mar. 2008. (Keyword) Streptococcus / protease / ClpP
207.	Atsushi Tabata, Souichirou Miyoshi, Ayuha Kadota, Kou Fukushima, Akiko Sukeno, Toshifumi Tomoyasu, Katsuhiko Hirota, Yoichiro Miyake, Hisashi Ohkuni and Hideaki Nagamune : 細菌感染反応場としてのヒト型CD59:ヒト細胞指向性コレステロール依存性細胞溶解毒素の受容体及びStreptococcus intermedius感染の宿主側トリガー因子としての役割, 第80回日本生化学会大会-第30回日本分子生物学会年会合同大会, Dec. 2007. (Keyword) Streptococcus / CD59 / Infection
208.	Hiroshima Riki, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが生産するヒト特異的細胞溶解毒素インターメディシンの発現調節, 第80回日本生化学会大会-第30回日本分子生物学会年会合同大会, Dec. 2007. (Keyword) Streptococcus / gene expression
209.	Toshifumi Tomoyasu, Syunsuke Azuma, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : 腸管出血性大腸菌のGrlAによるLEE1オペロンの新規発現調節機構, 第30回日本分子生物学会年会, Dec. 2007. (Keyword) EHEC / LEE pathgenisity island
210.	Shinohara Yuki, Takumi Ishida, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Analysis of intermolecular interaction site of intermedilysin, 第60回日本細菌学会中国四国支部総会, Oct. 2007. (Keyword) Streptococcus / Cytolysin
211.	Atsushi Tabata, Miyoshi Souichirou, Kadota Ayuha, Akiko Sukeno, Katsuhiko Hirota, Toshifumi Tomoyasu, Yoichiro Miyake and Hideaki Nagamune : Streptococcus intermedius が分泌する細胞溶解毒素インターメディリシンが関与するヒト細胞特異的な感染現象, 第54回毒素シンポジウム, Sep. 2007. (Keyword) cytotoxicity / Streptococcus
212.	Toshifumi Tomoyasu, Riki Hiroshima, Syunsuke Ishida, Akira Kominami, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusの病原性発現調節機構の解析, 第16回Lancefieldレンサ球菌研究会, Jun. 2007. (Keyword) Streptococcus / Pathogenisity / Chaperon
213.	Atsushi Tabata, 三好宗一郎, Toshifumi Tomoyasu, Katsuhiko Hirota, Yoichiro Miyake and Hideaki Nagamune : 細胞溶解毒素インターメディリシンのヒト細胞特異的感染因子としての役割, 第80回日本細菌学会総会, Mar. 2007.
214.	今木英統, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : GrlR，GrlAによる腸管出血性大腸菌(EHEC)のLEE領域発現制御機構の解析, 第80回日本細菌学会総会, Mar. 2007.
215.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : 腸管出血性大腸菌(EHEC)のLEE領域発現制御機構の解析, 第59回日本細菌学会中国・四国支部総, Oct. 2006.
216.	福島江, Atsushi Tabata, Toshifumi Tomoyasu, 大倉一人, 大国壽士 and Hideaki Nagamune : Sm-hPAFの受容体多様性:コレステロール依存性細胞溶解毒素の分子進化, 第59回日本細菌学会中国・四国支部総, Oct. 2006.
217.	Yuki Shinihara, 福島江, Toshifumi Tomoyasu, 大国壽士, 大倉一人 and Hideaki Nagamune : インターメディリシン及びそのホモローグの受容体認識部位の解析, 第79回日本細菌学会総会, Mar. 2006.
218.	Akira Kominami, Toshifumi Tomoyasu, Kou Fukushima and Hideaki Nagamune : ヒト特異的細胞溶解毒素インターメディリシンの発現調節機構の遺伝学的解析, 第79回日本細菌学会総会, Mar. 2006.
219.	Toshifumi Tomoyasu, 高屋明子, Hideaki Nagamune and 山本友子 : 腸管出血性大腸菌ClpXPプロテアーゼによるLEE pathogenic island 発現制御機構の解, 第79回日本細菌学会総会, Mar. 2006.

Et cetera, Workshop:

1.	Atsushi Tabata, YOKOHATA Shuto, 大倉一人, Toshifumi Tomoyasu and Hideaki Nagamune : ペプチド溶血毒素ストレプトリジンSの血液成分による安定化と病原性への寄与, 第53回レンサ球菌研究会, Jul. 2023.
2.	Atsushi Tabata, 安養寺夏希, 大久保行将, 北條恵子, 水品善之, Toshifumi Tomoyasu and Hideaki Nagamune : Development of surface-processing systems as targeting technology of nano-particles, --- Optimization of the transpeptidase reaction of bacterial sortase A using GFP-substrate panel and investigation for its applications ---, 神戸学院大学ライフサイエンス産学連携研究センター, Mar. 2014.
3.	Atsushi Tabata, 大久保行将, 安養寺夏希, Toshifumi Tomoyasu and Hideaki Nagamune : Development of surface-processing systems as targeting technology of nano-particles, --- Development and investigation of SrtA substrate-producing system for surface processing ---, 神戸学院大学ライフサイエンス産学連携研究センター, Mar. 2013.
4.	Atsushi Tabata, 大久保行将, Toshifumi Tomoyasu and Hideaki Nagamune : 標的細胞に対する汎用性を高めたDDSツールの構築とその機能に関する評価, 第16回バイオ治療法研究会学術集会, Dec. 2012.
5.	Toshifumi Tomoyasu, Ayumi Okamoto, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : ラクトースリプレッサーLacRによるインターメディリシン遺伝子の発現抑制, 第19回Lancefieldレンサ球菌研究会, Jun. 2010.
6.	Atsushi Tabata, 山本泰裕, Toshifumi Tomoyasu, Katsuhiko Hirota, Yoichiro Miyake, 大国寿士 and Hideaki Nagamune : 2種のコレステロール依存性細胞溶解毒素を産生する川崎病患児由来Streptococcus mitis Nm-65株の病原性に関する検討, 第19回Lancefieldレンサ球菌研究会, Jun. 2010.

Patent:

1.	Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Cholesterol-dependent cytolysin variant and use thereof in DDS, WO2012/121395 A1 (Sep. 2012), .

Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)

Molecular characteristics specific for streptolysin S produced by human opportunistic Anginosus group streptococci (Project/Area Number: 23K09139 )
The environmental determinant for Anginosus group streptococci to be the human pathogen. (Project/Area Number: 20K09919 )
Molecular evolution of hemolysins involved in oral streptococcal pathogenicity (Project/Area Number: 18K09552 )
Importance for the existence of mobile-genetic elements in cytotoxic Anginosus group streptococci (Project/Area Number: 17K11615 )
Pathogenicity acquisition mechanism of oral streptococci via gene transfer and expression of cytolysin genes (Project/Area Number: 15K11012 )
Role of a novel secreted glycosidase for pathogenicity of a human-specific pathogenic streptococci. (Project/Area Number: 26460528 )
Highly pathogenic Streptococcus mitis exists: A study on its pathogenicity and epidemiology (Project/Area Number: 24592769 )
Investigation of the regulatory mechanism for the production of a human specific cytolysin, a crucial factor for the infectivity of Streptococcus intermedius (Project/Area Number: 23590510 )
Development of a cancer treatment technique using intracellular collapsing liposomes directed to cancer with double safety systems (Project/Area Number: 21590115 )
Regulation of pathogenicity by the heat shock chaperone and the protease in streptococci (Project/Area Number: 19590449 )
Molecular mechanism of human-specific infection by an oral streptococcus, Streptococcusintermedius (Project/Area Number: 18592004 )
Expression control mechanisms of LEE pathogenic factors by AAA proteases in Enterohaemorrhagic and Enteropathogenic Eschericha coli (Project/Area Number: 17590387 )
Autophagy and strategy for intracellular multiplication of pathogenic bacteria (Project/Area Number: 17390125 )
Molecular mechanisms of intracellular growth of Salmonella (Project/Area Number: 16017218 )
Regulatory mechanisms of type III secretion system by molecular chaperones and proteases in Salmonella enterica serovar Typhimurium. (Project/Area Number: 15590055 )
サルモネラの食細胞内寄生性の分子機構 (Project/Area Number: 15019017 )
細菌感染における生体防御機構エスケープ因子としてのストレス蛋白の解析 (Project/Area Number: 13771371 )
Studies on Regulatory Mechanism of Salmonella Pathogenesis by Proteome Analysis (Project/Area Number: 13470058 )
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Associate Professor : Tomoyasu, Toshifumi

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Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)