2017 Fiscal Year Final Research Report
Analysis of the species-specific molecular mechanism of C. perfringens-specific lytic enzyme Psm and its application
Project/Area Number |
15K08482
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Bacteriology (including mycology)
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Research Institution | Matsuyama University |
Principal Investigator |
Tamai Eiji 松山大学, 薬学部, 准教授 (40333512)
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Co-Investigator(Kenkyū-buntansha) |
吉田 裕美 香川大学, 総合生命科学研究センター, 准教授 (10313305)
成谷 宏文 広島大学, 生物圏科学研究科, 准教授 (30452668)
|
Co-Investigator(Renkei-kenkyūsha) |
YOSHIDA Hiromi 香川大学, 総合生命科学研究センター, 准教授 (10313305)
|
Project Period (FY) |
2015-04-01 – 2018-03-31
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Keywords | 溶菌酵素 / ウエルシュ菌 |
Outline of Final Research Achievements |
In this study, molecular mechanism of Clostridium perfringens specific lytic enzyme (Psm, Acp, CPE 1138) and its application study were carried out. The species specificity of Psm was found to be in its cell wall binding domain. In addition, enteric coarted preparations of Psm showed some effect on C. perfringens in the intestine. Furthermore, in this study, it was clarified that the catalytic domain of Acp adopts a crescent structure composed of three subdomains, and revealed that the reaction mechanism is Neighboring - group mechanism. In addition, the catalytic domain and cell wall binding domain of CPE 1138 were identified. Furthermore, crystals of the catalytic domain of CPE 1138 were obtained, and data with resolution of 2.0 angstroms was successfully obtained by X-ray structural analysis. Currently, this structural analysis is carried out.
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Free Research Field |
細菌学
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