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Thromb Haemost 2004; 91(04): 779-789
DOI: 10.1160/TH03-05-0287
Wound Healing and Inflammation/Infection
Schattauer GmbH

Extracellular fibrinogen binding protein, Efb, from Staphylococcus aureus binds to platelets and inhibits platelet aggregation

Oonagh Shannon
1   Department of Laboratory Medicine, Karolinska Institutet, Stockholm, Sweden
,
Jan-Ingmar Flock
1   Department of Laboratory Medicine, Karolinska Institutet, Stockholm, Sweden
› Author AffiliationsFinancial support: This work was supported by grants from the Swedish Research Council (K2001-16X-12218-05C) and Biostapro AB.
Further Information

Publication History

Received 13 May 2003

Accepted after revision 06 January 2004

Publication Date:
06 December 2017 (online)

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Summary

S. aureus produces and secretes a protein, extracellular fibrinogen binding protein (Efb), which contributes to virulence in wound infection. We have shown here that Efb is a potent inhibitor of platelet aggregation. Efb can bind specifically to platelets by two mechanisms; 1) to fibrinogen naturally bound to the surface of activated platelets and 2) also directly to a surface localized component on the platelets. This latter binding of Efb is independent of fibrinogen. The specific binding of Efb to the putative receptor on the platelet surface results in a stimulated, non-functional binding of fibrinogen in a dose dependent manner, distinct from natural binding of fibrinogen to platelets. The natural binding of fibrinogen to GPIIb/IIIa on activated platelets could be blocked by a monoclonal antibody against this integrin, whereas the Efb-mediated fibrinogen binding could not be blocked. The enhanced Efb-dependent fibrinogen binding to platelets is of a nature that does not promote aggregation of the platelets; instead it inhibits aggregation. The anti-thrombotic action of Efb may explain the effect of Efb on wound healing, which is delayed in the presence of Efb.

Keywords

Bacteria - coagulation inhibitors - fibrinogen / fibrin - platelet physiology
 

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