[ODP6A] a. Adhesion Factors, and Colonization Factors

[ODP-120] Function of the autolysin of Clostridium perfringens

○Shogo Emi¹, Riyo Aono¹, Nozomu Matsunaga², Hirofumi Nariya³, Eiji Tamai⁴, Yasuo Hitsumoto², Seiichi Katayama² (¹Dept. Life Sci., Grad. Sch. Sci., Okayama Univ. Sci., ²Dept. Life Sci., Fac. Sci., Okayama Univ. Sci., ³Dept. Food Sci., Fac. Human Life., Jumonji Univ., ⁴Dept. Infect. Dis., Coll. Pharm., Matsuyama Univ.)

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.