Differences in the aromatic domain of homologous streptococcal fibronectin-binding proteins trigger different cell invasion mechanisms and survival rates.
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Graham, Rikki M
Talay, Susanne R
Chhatwal, Gursharan S
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AbstractGroup A streptococci (GAS, Streptococcus pyogenes) and Group G streptococci (GGS, Streptococcus dysgalactiae ssp. equisimilis) adhere to and invade host cells by binding to fibronectin. The fibronectin-binding protein SfbI from GAS acts as an invasin by using a caveolae-mediated mechanism. In the present study we have identified a fibronectin-binding protein, GfbA, from GGS, which functions as an adhesin and invasin. Although there is a high degree of similarity in the C-terminal sequence of SfbI and GfbA, the invasion mechanisms are different. Unlike caveolae-mediated invasion by SfbI-expressing GAS, the GfbA-expressing GGS isolate trigger cytoskeleton rearrangements. Heterologous expression of GfbA on the surface of a commensal Streptococcus gordonii and purified recombinant protein also triggered actin rearrangements. Expression of a truncated GfbA (lacking the aromatic domain) and chimeric GfbA/SfbI protein (replacing the aromatic domain of SfbI with the GfbA aromatic domain) on S. gordonii or recombinant proteins alone showed that the aromatic domain of GfbA is responsible for different invasion mechanisms. This is the first evidence for a biological function of the aromatic domain of fibronectin-binding proteins. Furthermore, we show that streptococci invading via cytoskeleton rearrangements and intracellular trafficking along the classical endocytic pathway are less persistence than streptococci entering via caveolae.
CitationDifferences in the aromatic domain of homologous streptococcal fibronectin-binding proteins trigger different cell invasion mechanisms and survival rates. 2011, 13 (3):450-68 Cell. Microbiol.
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- Identification of a fibronectin-binding protein (GfbA) in pathogenic group G streptococci.
- Authors: Kline JB, Xu S, Bisno AL, Collins CM
- Issue date: 1996 Jun
- The fibronectin binding domain of the Sfb protein adhesin of Streptococcus pyogenes occurs in many group A streptococci and does not cross-react with heart myosin.
- Authors: Valentin-Weigand P, Talay SR, Kaufhold A, Timmis KN, Chhatwal GS
- Issue date: 1994 Aug
- The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells.
- Authors: Molinari G, Talay SR, Valentin-Weigand P, Rohde M, Chhatwal GS
- Issue date: 1997 Apr
- Co-operative binding of human fibronectin to Sfbl protein triggers streptococcal invasion into respiratory epithelial cells.
- Authors: Talay SR, Zock A, Rohde M, Molinari G, Oggioni M, Pozzi G, Guzman CA, Chhatwal GS
- Issue date: 2000 Dec
- Host cell caveolae act as an entry-port for group A streptococci.
- Authors: Rohde M, Müller E, Chhatwal GS, Talay SR
- Issue date: 2003 May