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Streptococcal protein fog: A novel matrix adhesin interacting with colagen I in vivo.

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Author

Summary, in English

Group G streptococcus (GGS) is a human pathogen of emerging clinical significance. It causes skin and soft tissue infections, occasionally resulting in life-threatening conditions such as sepsis and necrotizing fasciitis. We recently identified FOG, a novel surface protein of GGS with fibrinogen binding and immune evasion properties. Here we investigated the role of FOG in streptococcal primary adhesion to host tissue. A FOG-expressing clinical isolate adhered more efficiently to human skin biopsies ex vivo and to the murine dermis in vivo than a FOG-deficient strain. Scanning and transmission electron microscopy of skin specimens exhibited that this property was assigned to the ability of FOG to interact with collagen I, a major interstitial component of the dermis. Overlay experiments with human skin extracts and radiolabeled FOG followed by matrix-assisted laser desorption/ionization time of flight mass spectrometry analysis identified both the alpha 1- and alpha 2-chains of collagen I as targets for FOG. Transmission electron microscopy of the molecular complexes revealed thread-like FOG molecules binding via their NH2 termini to distinct sites on collagen I monomers and fibrils. The results demonstrate that FOG is important for GGS adhesion in vivo, implying a pathogenic role for this surface protein.

Publishing year

2006

Language

English

Pages

1670-1679

Publication/Series

Journal of Biological Chemistry

Volume

281

Issue

3

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Other Clinical Medicine
  • Infectious Medicine

Status

Published

ISBN/ISSN/Other

  • ISSN: 1083-351X