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

Nitsche, Patric LU ; Linge, Helena LU ; Frick, Inga-Maria LU and Mörgelin, Matthias LU (2006) In Journal of Biological Chemistry 281(3). p.1670-1679
Abstract
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... (More)
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. (Less)
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author
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type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
281
issue
3
pages
1670 - 1679
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • pmid:16278217
  • wos:000234652000047
  • scopus:33644968057
ISSN
1083-351X
DOI
10.1074/jbc.M506776200
language
English
LU publication?
yes
id
b3fd471d-f12f-4df8-adf2-e32e687d13da (old id 148029)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16278217&dopt=Abstract
date added to LUP
2016-04-01 12:13:51
date last changed
2022-03-28 22:02:23
@article{b3fd471d-f12f-4df8-adf2-e32e687d13da,
  abstract     = {{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.}},
  author       = {{Nitsche, Patric and Linge, Helena and Frick, Inga-Maria and Mörgelin, Matthias}},
  issn         = {{1083-351X}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{1670--1679}},
  publisher    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{Journal of Biological Chemistry}},
  title        = {{Streptococcal protein fog: A novel matrix adhesin interacting with colagen I in vivo.}},
  url          = {{https://lup.lub.lu.se/search/files/2837122/625162.pdf}},
  doi          = {{10.1074/jbc.M506776200}},
  volume       = {{281}},
  year         = {{2006}},
}