2023 Fiscal Year Final Research Report
Functions of the fibronectin-binding proteins and pili from Clostridium perfringens
| Project/Area Number |
20K07503
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Review Section |
Basic Section 49050:Bacteriology-related
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| Research Institution | Okayama University of Science |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
松永 望 岡山理科大学, 理学部, 講師 (30780142)
櫃本 泰雄 岡山理科大学, 理学部, 教授 (90136333)
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| Project Period (FY) |
2020-04-01 – 2024-03-31
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| Keywords | Clostridium perfringens / fibronectin (Fn) / Fn-binding protein / autolysin / GAPDH / pili |
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| Outline of Final Research Achievements |
Clostridium perfringens cells bind to the human fibronectin (Fn) molecules. Autolysin (acp), an autolysing enzyme of this bacterium, has Fn-binding activity, and the complementation experiments of the acp gene have revealed that it is the Fn receptor of Clostridium perfringens. glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was also shown to bind Fn and plasminogen. Other Fn-binding proteins, FbpC and FbpD, were shown not to be involved in Welsh Fn binding. However, FbpD was suggested to have peptidoglycan-degrading activity. As for the pili, the process of lineage formation by its compotent proteins, CppA and CppB, and the sortase C that links them, is schematically shown.
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| Free Research Field |
細菌学
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| Academic Significance and Societal Importance of the Research Achievements |
ウェルシュ菌（Clostridium perfringens）は、ヒトにガス壊疽と食中毒を引きおこす病原菌である。この細菌は、創傷感染する際、まずフィブロネクチンなどの細胞外マトリックスタンパク質に結合することが必要になる。今回の科学研究費の支援によって、我々は、ウェルシュ菌の菌体表層に存在するフィブロネクチンレセプタータンパク質が、自己溶解酵素オートリシンであることを見出した。さらに他の付着因子と考えられている線毛の形成過程を模式的に示した。これらの発見は、ウェルシュ菌の宿主組織への付着のメカニズムを明らかにするもので学術的に意義があると考えられた。
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