Streptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
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.
CitationJ. Biol. Chem. 2006, 281(3):1670-9
- Protein FOG--a streptococcal inhibitor of neutrophil function.
- Authors: Johansson HM, Mörgelin M, Frick IM
- Issue date: 2004 Dec
- Group G streptococcal IgG binding molecules FOG and protein G have different impacts on opsonization by C1q.
- Authors: Nitsche-Schmitz DP, Johansson HM, Sastalla I, Reissmann S, Frick IM, Chhatwal GS
- Issue date: 2007 Jun 15
- Protein FOG is a moderate inducer of MIG/CXCL9, and group G streptococci are more tolerant than group A streptococci to this chemokine's antibacterial effect.
- Authors: Linge HM, Sastalla I, Nitsche-Schmitz DP, Egesten A, Frick IM
- Issue date: 2007 Nov
- Monoclonal antibodies recognizing the Enterococcus faecalis collagen-binding MSCRAMM Ace: conditional expression and binding analysis.
- Authors: Hall AE, Gorovits EL, Syribeys PJ, Domanski PJ, Ames BR, Chang CY, Vernachio JH, Patti JM, Hutchins JT
- Issue date: 2007 Aug-Sep
- Streptococcus pyogenes collagen type I-binding Cpa surface protein. Expression profile, binding characteristics, biological functions, and potential clinical impact.
- Authors: Kreikemeyer B, Nakata M, Oehmcke S, Gschwendtner C, Normann J, Podbielski A
- Issue date: 2005 Sep 30