Differences in the aromatic domain of homologous streptococcal fibronectin-binding proteins trigger different cell invasion mechanisms and survival rates.

2.50
Hdl Handle:
http://hdl.handle.net/10033/347148
Title:
Differences in the aromatic domain of homologous streptococcal fibronectin-binding proteins trigger different cell invasion mechanisms and survival rates.
Authors:
Rohde, Manfred ( 0000-0003-0522-3580 ) ; Graham, Rikki M; Branitzki-Heinemann, Katja; Borchers, Patricia; Preuss, Claudia; Schleicher, Ina; Zähner, Dorothea; Talay, Susanne R; Fulde, Marcus; Dinkla, Katrin; Chhatwal, Gursharan S
Abstract:
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 microbiology
Issue Date:
Mar-2011
URI:
http://hdl.handle.net/10033/347148
DOI:
10.1111/j.1462-5822.2010.01547.x
PubMed ID:
21054741
Type:
Article
Language:
en
ISSN:
1462-5822
Appears in Collections:
Publications of Dept. Medizinische Mikrobiologie (MMIK)

Full metadata record

DC FieldValue Language
dc.contributor.authorRohde, Manfreden
dc.contributor.authorGraham, Rikki Men
dc.contributor.authorBranitzki-Heinemann, Katjaen
dc.contributor.authorBorchers, Patriciaen
dc.contributor.authorPreuss, Claudiaen
dc.contributor.authorSchleicher, Inaen
dc.contributor.authorZähner, Dorotheaen
dc.contributor.authorTalay, Susanne Ren
dc.contributor.authorFulde, Marcusen
dc.contributor.authorDinkla, Katrinen
dc.contributor.authorChhatwal, Gursharan Sen
dc.date.accessioned2015-03-26T09:52:40Zen
dc.date.available2015-03-26T09:52:40Zen
dc.date.issued2011-03en
dc.identifier.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.en
dc.identifier.issn1462-5822en
dc.identifier.pmid21054741en
dc.identifier.doi10.1111/j.1462-5822.2010.01547.xen
dc.identifier.urihttp://hdl.handle.net/10033/347148en
dc.description.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.en
dc.language.isoenen
dc.subject.meshActinsen
dc.subject.meshAdhesins, Bacterialen
dc.subject.meshBacterial Adhesionen
dc.subject.meshCaveolaeen
dc.subject.meshCell Lineen
dc.subject.meshCytoskeletonen
dc.subject.meshEndocytosisen
dc.subject.meshFibronectinsen
dc.subject.meshHumansen
dc.subject.meshLysosomesen
dc.subject.meshMicroscopy, Electronen
dc.subject.meshMicroscopy, Fluorescenceen
dc.subject.meshPhagocytosisen
dc.subject.meshPolymerase Chain Reactionen
dc.subject.meshRecombinant Fusion Proteinsen
dc.subject.meshStreptococcusen
dc.subject.meshStreptococcus gordoniien
dc.subject.meshStreptococcus pyogenesen
dc.titleDifferences in the aromatic domain of homologous streptococcal fibronectin-binding proteins trigger different cell invasion mechanisms and survival rates.en
dc.typeArticleen
dc.identifier.journalCellular microbiologyen

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