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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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Contribution to journal
publication status
published
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in
Journal of Biological Chemistry
volume
281
issue
3
pages
1670 - 1679
publisher
ASBMB
external identifiers
  • pmid:16278217
  • wos:000234652000047
  • scopus:33644968057
ISSN
1083-351X
DOI
10.1074/jbc.M506776200
language
English
LU publication?
yes
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b3fd471d-f12f-4df8-adf2-e32e687d13da (old id 148029)
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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
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2021-04-13 03:14:48
@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    = {ASBMB},
  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/ws/files/2837122/625162.pdf},
  doi          = {10.1074/jbc.M506776200},
  volume       = {281},
  year         = {2006},
}