Adhesive properties of Clostridium perfringens to extracellular matrix proteins collagens and fibronectin

•Clostridium perfringens interacted with collagens through prebound fibronectin (Fn).•Fn-binding proteins inhibited C. perfringens from binding to Fn-prebound collagen.•Fn-binding proteins bound to the surface of C. perfringens cells.

The adhesive properties of Clostridium perfringens to collagens, gelatin, fibronectin (Fn), Fn-prebound collagens, and Fn-prebound gelatin were investigated. C. perfringens could bind to Fn-prebound collagen type II, type III, and gelatin, but not to gelatin or collagens except for collagen type I directly. Recombinant Fn-binding proteins of C. perfringens, rFbpA and rFbpB, were used to examine Fn-mediated bacterial adherence to collagen type I. In the presence of rFbps, C. perfringens adherence to Fn-prebound collagen type I was inhibited in a dose-dependent manner. Fn was not released from the coated collagen type I by the presence of rFbps, and rFbps did not bind to collagen type I. Thus, the inhibition of C. perfringens binding to Fn-prebound collagen type I by rFbps could not be explained by the removal of Fn from collagen or by the competitive binding of rFbps to collagen. Instead, both rFbps were found to bind to C. perfringens. These results suggest the possibility that rFbps may bind to the putative Fn receptor expressed on C. perfringens and competitively inhibit Fn binding to C. perfringens.