Structural and functional analysis of the tandem B-zipper interaction of a streptococcal protein with human fibronectin

  • Norris N
  • Bingham R
  • Harris G
 et al. 
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Abstract

Bacterial fibronectin-binding proteins (FnBPs) contain a large intrinsically disordered region (IDR) that mediates adhesion of bacteria to host tissues, and invasion of host cells, through binding to fibronectin (Fn). These FnBP IDRs consist of Fn-binding repeats (FnBRs) that form a highly extended tandem β-zipper interaction on binding to the N-terminal domain of Fn. Several FnBR residues are highly conserved across bacterial species, and here we investigate their contribution to the interaction. Mutation of these residues to alanine in SfbI-5 (a disordered FnBR from the human pathogen Streptococcus pyogenes) reduced binding, but for each residue the change in free energy of binding was

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Authors

  • Nicole C. Norris

  • Richard J. Bingham

  • Gemma Harris

  • Adrian Speakman

  • Richard P O Jones

  • Andrew Leech

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