2.50
Hdl Handle:
http://hdl.handle.net/10033/14732
Title:
Streptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo.
Authors:
Nitsche, D Patric; Johansson, Helena M; Frick, Inga-Maria; Mörgelin, Matthias
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 alpha1- and alpha2-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.
Citation:
J. Biol. Chem. 2006, 281(3):1670-9
Issue Date:
20-Jan-2006
URI:
http://hdl.handle.net/10033/14732
DOI:
10.1074/jbc.M506776200
PubMed ID:
16278217
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
Publications of Dept. Medizinische Mikrobiologie (MMIK)

Full metadata record

DC FieldValue Language
dc.contributor.authorNitsche, D Patric-
dc.contributor.authorJohansson, Helena M-
dc.contributor.authorFrick, Inga-Maria-
dc.contributor.authorMörgelin, Matthias-
dc.date.accessioned2007-11-26T10:18:16Z-
dc.date.available2007-11-26T10:18:16Z-
dc.date.issued2006-01-20-
dc.identifier.citationJ. Biol. Chem. 2006, 281(3):1670-9en
dc.identifier.issn0021-9258-
dc.identifier.pmid16278217-
dc.identifier.doi10.1074/jbc.M506776200-
dc.identifier.urihttp://hdl.handle.net/10033/14732-
dc.description.abstractGroup 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 alpha1- and alpha2-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.en
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dc.titleStreptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo.en
dc.typeArticleen
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