| Project/Area Number |
15K08481
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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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| Research Field |
Bacteriology (including mycology)
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| Research Institution | Okayama University of Science |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
櫃本 泰雄 岡山理科大学, 理学部, 教授 (90136333)
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| Project Period (FY) |
2015-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2018: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2017: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2016: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | Clostridium perfringens / fibronectin (Fn) / Fn-binding protein（Fbp) / GAPDH / autolysin (Acp) / Fn-binding proteins / autolysin / Fn-binding protein / ウェルシュ菌 / ガス壊疽 / フィブロネクチン (Fn) / Fn結合タンパク質 |
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| Outline of Final Research Achievements |
Clostridium perfringens is a Gram-positive, spore-forming anaerobic bacterium, causing gas gangrene and food poisoning in humans and animals. It is thought that C. perfringens entering the wound binds to human fibronectin (Fn) molecules in connective tissue, and colonizes.
In this work, it was shown that C. perfringens cells bound to III9 and III10 fragments of Fn. This suggests that the bacterium retains fibronectin-binding protein(s) (Fbp) on the cell surface. In fact, some Fbps were isolated by treating the cell with endolysin, a cell wall degrading enzyme. Some of these proteins were identified as FbpC (56 kDa; CPE0625), FbpD (45 kDa; CPE0630), and glyceraldehyde -3-phosphate dehydrogenase (GAPDH; CPE1304). It was also shown that GAPDH binds to autolysin (Acp; CPE1231), a lytic enzyme present on the cell surface. These results suggest that many proteins might be involved in the Fn binding of C. perfringens cells.
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| Academic Significance and Societal Importance of the Research Achievements |
ウェルシュ菌(C. perfringens)によるガス壊疽の発生は少ないが、急速に敗血症まで進行し致死的となることがある。その侵入門戸は、傷口である。侵入した細菌は、結合組織内の Fnを認識し結合することにより定着すると考えられる。この定着の分子メカニズムは今までほとんど不明であった。本研究の成果により、ウェルシュ菌は、Fn分子の一部分を特異的に認識しており、その認識には、菌体表層に存在する複数のFbpが関わっている可能性が明らかとなった。さらに、どのFbpがウェルシュ菌の定着に主要な貢献をするのか明らかになれば、この感染症に対する防御の具体的なアイデアが生まれることに繋がると考えている。
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