講演・口頭発表等

基本情報

氏名 片山 誠一
氏名(カナ) カタヤマ セイイチ
氏名(英語) Katayama Seiichi
所属 生命科学部 医療技術学科
職名 教授
researchmap研究者コード 1000052332
researchmap機関 岡山理科大学

タイトル

ウェルシュ菌の細胞表面上のフィブロネクチン受容体としてのオートリシン

講演者

Seiichi Katayama, Riyo Aono, Shogo Emi, Kanako Okabe-Watanabe, Hirofumi Nariya, Nozomu Matsunaga, Yasuo Hitsumoto

会議名

The 13th International Conference on the Molecular Biology and Pathogenesis of the Clostridia (ClostPath13)

開催年月日

2023/09/20

招待の有無

無し

記述言語

英語

発表種類

学会講演(シンポジウム・セミナー含む)

会議区分

国際会議

会議種別

ポスター発表

主催者

The International Conference on the Molecular Biology and Pathogenesis of the Clostridia

開催地

Banff, Canada

URL

概要

Clostridium perfringens is an obligate anaerobe that causes food poisoning and gas gangrene. C. perfringenscells adhere to collagen via fibronectin (Fn) [1]. In this study, we found that a peptidoglycan hydrolase of C. perfringens, i.e., autolysin (Acp), has Fn-binding activity. Acp is a 120-kD polypeptide containing 10 cell wall-binding repeats at the N terminus and one catalytic domain (AcpCD) at the C terminus [2]. By a binding assay using recombinant Acp fragments, Fn was found to bind to the AcpCD. Fn binding was significantly decreased in mutant cells lacking Acp (strain 13 acp::erm), but was restored by the complementation of the acp gene.Three kinds of Fn-binding proteins (FbpC, FbpD, and glyceraldehyde-3-phosphate dehydrogenase) are known in C. perfringens [3]. There was no difference in Fn-binding activity between the mutant cells (SAK3) lacking both FbpC and FbpD and the wild-type cells, indicating that these Fnbinding proteins are not involved in Fn binding to C. perfringens cells. These results suggest that Acp is an Fn receptor on the surface of C. perfringens cells.

[1] Hitsumoto Y, et al. Adhesive properties of Clostridium perfringens to extracellular matrix proteins collagens and fibronectin. Anaerobe 2014. 25:67-71. [2] Camiade E, et al. Characterization of Acp, a peptidoglycan hydrolase of Clostridium perfringens with N-acetylglucosaminidase activity that is implicated in cell separation and stressinduced autolysis. J Bacteriol. 2010. 192:2373-2384. [3] Katayama S, et al. Novel cell wall−associated fibronectin-binding proteins of Clostridium perfringens. Int J Anal Bio-Sci. 2015. 3: 1-9.