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Blood, 15 July 2002, Vol. 100, No. 2, pp. 509-516
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
A role for glycoprotein Ib in Streptococcus
sanguis-induced platelet aggregation
Steven W. Kerrigan,
Ian Douglas,
Ann Wray,
Jason Heath,
Michael F. Byrne,
Desmond Fitzgerald, and
Dermot Cox
From the Department of Clinical Pharmacology, Royal
College of Surgeons in Ireland, Dublin, Ireland, and Department of Oral
Pathology, School of Clinical Dentistry, University of Sheffield,
Sheffield, United Kingdom.
Numerous studies have implicated bacteria in cardiovascular
disease, but there is a paucity of information on the mechanism involved. In this study we show how the common oral bacterium Streptococcus sanguis can directly interact with platelets,
resulting in activation and aggregate formation. Platelet aggregation
was dependent on glycoprotein IIb/IIIa (GPIIb/IIIa) and thromboxane. Platelets could also directly bind to S sanguis, but this
interaction was not inhibited by GPIIb/IIIa antagonists. Antibodies to
GPIb could inhibit both platelet aggregation and platelet adhesion to
bacteria. This suggested a direct interaction between GPIb and S
sanguis; however, this interaction did not require von Willebrand factor, the normal ligand for GPIb. By use of a range of monoclonal antibodies to GPIb and the enzyme mocharagin, which cleaves GPIb at
amino acid 282, the interaction was localized to a region within the
N-terminal 1-225 portion of GPIb . Furthermore S sanguis
failed to induce aggregation of platelets from a patient with
Bernard-Soulier disease, the organism bound to Chinese hamster ovary
cells transfected with the GPIb gene but did not bind to
mock-transfected cells and biotin-labeled S sanguis cells
bound to purified GPIb in ligand blots. It is suggested that the
interaction between S sanguis and GPIb is important in the
pathogenesis of infective endocarditis and may also play a contributory
role in some cases of myocardial infarction.
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