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

Ulrich Schwarz-Linek, MJ Plevin, AR Pickford, M Hook, ID Campbell, JR Potts

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

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. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Original languageEnglish
Pages (from-to)137-140
Number of pages4
JournalFEBS Letters
Volume497
Issue number2-3
DOIs
Publication statusPublished - 25 May 2001

Keywords

  • biomolecular nuclear magnetic resonance
  • fibronectin
  • microbial surface component recognizing adhesive matrix molecules
  • protein-protein interaction
  • STAPHYLOCOCCUS-AUREUS
  • NMR-SPECTROSCOPY
  • HETERONUCLEAR NMR
  • CROSS-RELAXATION
  • H-1-NMR SPECTRA
  • PROTEINS
  • ELUCIDATION
  • ASSIGNMENT
  • COHERENCE
  • ADHERENCE

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