Differences in the aromatic domain of homologous streptococcal fibronectin-binding proteins trigger different cell invasion mechanisms and survival rates.
Name:
rohde-graham et al_final.pdf
Size:
2.519Mb
Format:
PDF
Description:
Open Access publication
Average rating
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.
Star rating
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Authors
Rohde, ManfredGraham, Rikki M
Branitzki-Heinemann, Katja
Borchers, Patricia
Preuss, Claudia
Schleicher, Ina
Zähner, Dorothea
Talay, Susanne R
Fulde, Marcus
Dinkla, Katrin
Chhatwal, Gursharan S
Issue Date
2011-03
Metadata
Show full item recordAbstract
Group 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.Citation
Differences 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.Journal
Cellular microbiologyPubMed ID
21054741Type
ArticleLanguage
enISSN
1462-5822ae974a485f413a2113503eed53cd6c53
10.1111/j.1462-5822.2010.01547.x
Scopus Count
The following license files are associated with this item:
Related articles
- 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
- 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
- Fc-mediated nonspecific binding between fibronectin-binding protein I of Streptococcus pyogenes and human immunoglobulins.
- Authors: Medina E, Molinari G, Rohde M, Haase B, Chhatwal GS, Guzmán CA
- Issue date: 1999 Sep 15
- Fibronectin-binding protein gene recombination and horizontal transfer between group A and G streptococci.
- Authors: Towers RJ, Gal D, McMillan D, Sriprakash KS, Currie BJ, Walker MJ, Chhatwal GS, Fagan PK
- Issue date: 2004 Nov