Differences in the aromatic domain of homologous streptococcal fibronectin-binding proteins trigger different cell invasion mechanisms and survival rates.
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
Graham, Rikki M
Talay, Susanne R
Chhatwal, Gursharan S
MetadataShow full item record
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.
The following license files are associated with this item:
- 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
- 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
- Streptococcus pyogenes recruits collagen via surface-bound fibronectin: a novel colonization and immune evasion mechanism.
- Authors: Dinkla K, Rohde M, Jansen WT, Carapetis JR, Chhatwal GS, Talay SR
- Issue date: 2003 Feb
- 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