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Blood, 1 February 2005, Vol. 105, No. 3, pp. 1052-1059. Prepublished online as a Blood First Edition Paper on September 21, 2004; DOI 10.1182/blood-2004-06-2149. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-06-2149v1 105/3/1052    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Pietrocola, G. Articles by Speziale, P. Search for Related Content PubMed PubMed Citation Articles by Pietrocola, G. Articles by Speziale, P. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY FbsA, a fibrinogen-binding protein from Streptococcus agalactiae, mediates platelet aggregation Giampiero Pietrocola, Axel Schubert, Livia Visai, Mauro Torti, J. Ross Fitzgerald, Timothy J. Foster, Dieter J. Reinscheid, and Pietro Speziale From the University of Pavia, Department of Biochemistry, Pavia, Italy; Department of Microbiology and Biotechnology, University of Ulm, Ulm, Germany; and Microbiology Department, Moyne Institute of Preventive Medicine, Trinity College, Dublin, Ireland. The bacterium Streptococcus agalactiae is an etiologic agent in the pathogenesis of endocarditis in humans. FbsA, a fibrinogen-binding protein produced by this pathogen, is considered an important virulence factor. In the present study we provide evidence that S agalactiae clinical isolates bearing FbsA attach to fibrinogen and elicit a fibrinogen-dependent aggregation of platelets. Mutants of S agalactiae lacking the fbsA gene lost the ability to attach to fibrinogen and to aggregate platelets. Plasmid-mediated expression of fbsA restored the capability for fibrinogen binding and platelet aggregation in S agalactiae fbsA mutants, and allowed Lactococcus lactis to interact with fibrinogen and to aggregate human platelets. Moreover, a monoclonal anti-FbsA antibody inhibited bacterial adherence to fibrinogen and S agalactiae–induced platelet aggregation. Platelet aggregation was inhibited by aspirin, prostaglandin E1, the peptide RGDS, and the antibody abciximab, demonstrating the specificity of platelet aggregation by S agalactiae and indicating an involvement of integrin glycoprotein IIb/IIIa in the induction of platelet aggregation. Aggregation was also dependent on anti-FbsA IgG and could be inhibited by an antibody against the platelet FcRIIA receptor. These findings indicate that FbsA is a crucial factor in S agalactiae–induced platelet aggregation and may therefore play an important role in S agalactiae–induced endocarditis. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: U. Samen, B. J. Eikmanns, D. J. Reinscheid, and F. Borges The Surface Protein Srr-1 of Streptococcus agalactiae Binds Human Keratin 4 and Promotes Adherence to Epithelial HEp-2 Cells Infect. Immun., November 1, 2007; 75(11): 5405 - 5414. [Abstract] [Full Text] [PDF] T. Tenenbaum, C. Bloier, R. Adam, D. J. Reinscheid, and H. Schroten Adherence to and Invasion of Human Brain Microvascular Endothelial Cells Are Promoted by Fibrinogen-Binding Protein FbsA of Streptococcus agalactiae Infect. Immun., July 1, 2005; 73(7): 4404 - 4409. [Abstract] [Full Text] [PDF]

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