Binding of a peptide from a Streptococcus dysgalactiae MSCRAMM to the N-terminal F1 module pair of human fibronectin involves both modules

Host invasion by a number of pathogenic bacteria such as staphylococci and streptococci involves binding to fibronectin, a ubiquitous extracellular ma trix protein. On the bacterial side, host extracellular matrix adherence is mediated by MSCRAMMs (microbial surface components recognizing adhesive ma trix molecules) which, in some cases, have been identified to be important virulence factors. In this study we used nuclear magnetic resonance spectro scopy to characterize the interaction of B3, a synthetic peptide derived fr om an adhesin of Streptococcus dysgalactiae, with the N-terminal module pai r (1)F1(2)F1 of human fibronectin. (1)F1(2)F1 chemical shift changes occurr ing on formation of the (1)F1(2)F1/B3 complex indicate that both modules bi nd to the peptide and that a similar region of each module is involved, A s imilar surface of the (4)F1(5)F1 module pair had previously been identified as the binding site for a fibronectin-binding peptide from Staphylococcus aureus. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.