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Binding of a peptide from a Streptococcus dysgalactiae MSCRAMM to the N‐terminal F1 module pair of human fibronectin involves both modules
Author(s) -
Schwarz-Linek Ulrich,
Plevin Michael J.,
Pickford Andrew R.,
Höök Magnus,
Campbell Iain D.,
Potts Jennifer R.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02418-8
Subject(s) - fibronectin , bacterial adhesin , streptococcus dysgalactiae , extracellular matrix , peptide , bacteria , biology , microbiology and biotechnology , virulence , peptide sequence , extracellular , binding site , staphylococcus aureus , streptococcus , biochemistry , genetics , gene , streptococcus agalactiae
Host invasion by a number of pathogenic bacteria such as staphylococci and streptococci involves binding to fibronectin, a ubiquitous extracellular matrix protein. On the bacterial side, host extracellular matrix adherence is mediated by MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) which, in some cases, have been identified to be important virulence factors. In this study we used nuclear magnetic resonance spectroscopy to characterize the interaction of B3, a synthetic peptide derived from an adhesin of Streptococcus dysgalactiae , with the N‐terminal module pair 1 F1 2 F1 of human fibronectin. 1 F1 2 F1 chemical shift changes occurring on formation of the 1 F1 2 F1/B3 complex indicate that both modules bind to the peptide and that a similar region of each module is involved. A similar 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 .