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

U Schwarz-Linek, Michael John Plevin, A R Pickford, M Höök, I D Campbell, J R Potts

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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 1F12F1 of human fibronectin. 1F12F1 chemical shift changes occurring on formation of the 1F12F1/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 4F15F1 module pair had previously been identified as the binding site for a fibronectin-binding peptide from Staphylococcus aureus.
Original languageEnglish
Pages (from-to)137-40
Number of pages4
JournalFEBS Letters
Issue number2-3
Publication statusPublished - 2001


  • Adhesins, Bacterial
  • Amino Acid Sequence
  • Bacterial Adhesion
  • Bacterial Proteins
  • Binding Sites
  • Calorimetry
  • Fibronectins
  • Host-Parasite Interactions
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments
  • Protein Binding
  • Protein Structure, Secondary
  • Streptococcus

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