A C-type lectin-like protein from Agkistrodon acutus venom binds to both platelet glycoprotein Ib and coagulation factor IX/factor X.

Agkisacutacin, a C-type lectin-like protein (CLP) isolated from Agkistrodon acutus venom, had been previously identified as an antagonist of platelet aggregation induced by ristocetin, as well as a certain extent fibrinogenlytic activity. In this study, agkisacutacin was further purified by three-step chromatography, and its biological functions were characterized. Agkisacutacin after further purification retained the effect on ristocetin-induced, von Willebrand factor-dependent platelet aggregation, while it lost the fibrinogenlytic activity. FACS and ELISA assays showed that agkisacutacin belongs to membrane glycoprotein Ib-binding protein (GPIb-bp) for it could block and inhibit the binding of anti-GPIb antibody to GPIb. Especially, agkisacutacin exhibits anti-coagulant activity and the function as IX/X-binding protein was confirmed by PAGE and ELISA. So, agkisacutacin is the first reported CLP that binds to both platelet membrane receptors and coagulation factors.