Autolysin as a fibronectin receptor on the cell surface of Clostridium perfringens

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

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

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

Banff, Canada

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.

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