Fibronectin-binding proteins of Clostridium perfringens recognize the III1-C fragment of fibronectin
Article first published online: 5 APR 2010
© 2010 The Societies and Blackwell Publishing Asia Pty Ltd
Microbiology and Immunology
Volume 54, Issue 4, pages 221–227, April 2010
How to Cite
Yamasaki, T., Hitsumoto, Y., Katayama, S. and Nogami, Y. (2010), Fibronectin-binding proteins of Clostridium perfringens recognize the III1-C fragment of fibronectin. Microbiology and Immunology, 54: 221–227. doi: 10.1111/j.1348-0421.2009.00201.x
- Issue published online: 5 APR 2010
- Article first published online: 5 APR 2010
- Received 24 July 2009; revised 13 November 2009; accepted 25 November 2009.
- Clostridium perfringens;
- fibronectin binding protein
The Clostridium perfringens strain 13 genome contains two genes (fbpA, fbpB) that encode putative Fbp. Both rFbpA and rFbpB were purified and their reactivity with human serum Fn was analyzed. To determine the region of the Fn molecule recognized by rFbp, a plate binding assay using N-terminal 70-kDa peptide, III1-C peptide, and 110-kDa peptide containing III2–10 of Fn was performed. Both rFbp bound to the III1-C peptide of Fn but not to the other peptides. However, the III1-C fragment of Fn is known to be cryptic in serum Fn. Then, rFbp-BP from Fn were purified by rFbp-affinity chromatography. The yield of purified proteins was approximately 1% of the applied Fn on a protein basis. Western blotting analysis of the rFbp-BP, using four different anti-Fn monoclonal antibodies, revealed that the rFbp-BP carried partial Fn antigenicity. Bindings of rFbp to rFbp-BP were inhibited by the presence of the III1-C peptide, suggesting that rFbp-BP express the III1-C fragment. The binding of Fn to III1-C was inhibited by the presence of either rFbpA or rFbpB. This result that suggests C. perfringens Fbps may inhibit the formation of Fn-matrix in vivo.