Study on structural biology of novel fibronectin-binding proteins of a pathogenic bacterium

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Clostridium perfringens is a pathogenic bacterium, causing gas gangrene and food poisoning in humans and animals. During the beginning of the infection, the bacteria formed colonies after the adhesion to wounds and epithelial cells of intestine. C. perfringens have proteins, FbpA (25 kDa, 220 aa) and FbpB (66 kDa, 575 aa) that bind to fibronectin in human. Therefore, this bacterium is thought to colonize after its Fn-binding.In this study, we indicated that Fn molecules bound to the C-terminal region of FbpA. An improved method of purification of recombinant FbpA was established to get a great quantity of the protein for crystallization. In addition, we found that both FbpA and FbpB could bind to the surface of C. perfringens cell. The studies on the structures and functions of the Fbps might lead to the development of protection against C. perfringens infection in the future.