[ODP6A] a. 接着因子・定着因子

[ODP-120] ウェルシュ菌の溶菌酵素オートリシンの機能解析

○江見 尚悟¹，青野 りよ¹，松永 望²，成谷 宏文³，玉井 栄治⁴，櫃本 泰雄²，片山 誠一² (¹岡山理科大院・理・臨床生命科学，²岡山理科大・理・臨床生命科学，³十文字大学・人間生活・食品開発学，⁴松山大学・薬・感染症)

Clostridium perfringens is a Gram-positive anaerobe, causing gas gangrene and food poisoning for humans. Human fibronectin (Fn) binds to the bacterial cells. We have found some Fn-binding proteins ‍including FbpC, FbpD, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH, CPE1304) in the peptidoglycan layers of C. perfringens cells. Recently, we found that Fn bound to the autolysin (Acp, CPE1231). Acp is a peptidoglycan hydrorase with an N-acetylglucosaminidase acitivity in the peptidoglycan layer of the cells. In this work, to investigate the other function of the autolysin, a null mutant (C. perfringens strain 13 acp::erm) were given from Dr. Bruno Dupuy (Pasteur Institute). The Fn-binding activity to the acp::erm cells decreased compared to that of strain 13 cells significantly. In order to comfirm this, the acp gene was cloned downstream a xylose-inducible promoter (xylRO) and the complementation tests with pxylRO-acp were performed. The Fn-binding activity to the acp::erm/pxylRO-acp cells recovered to that of the strain 13 in the presence of 4% xylose. Interestingly, the amount of GAPDH on the surface of the the acp::erm cells also decreased, and recovered by the same complementation test. These results suggested that Acp on the cell surface might interact with GAPDH and that both Acp and GAPDH might be involved in the Fn-binding to C. perfringens cells.