A novel 25 kDa protein from the venom of Bitis arietans with similarity to C-type lectins causes fibrinogen-dependent platelet agglutination.

Snake venoms affect blood coagulation and platelet functions in various ways. Venom from the Viperidae and Crotalidae family of snakes contains biologically active proteins that possess coagulant and anticoagulant activities, as well as platelet aggregating and inhibitory activities. Many of these proteins belong to the C-type lectin family. C-type lectins from viper venoms can act by prohibiting the interaction between platelet receptors, such as GPIIbIIIa and the GPIb/V/IX complex, and their ligands. We report on the purification of a novel 25 kDa protein, Ba25, from Bitis arietans with a primary structure that possesses similarity to other C-type lectins from viper venom. This protein has a profound effect on the clotting of whole blood, as well as being able to cause agglutination of platelets in platelet rich plasma without degranulation of the cells, but not of washed platelets in the absence of fibrinogen. Ba25 interacts with the platelet via the GPIb/V/IX, as well as the GPIIbIIIa receptor, and causes an increase in binding of fibrinogen to platelets. These results suggest that Ba25 may be a potent mediator of platelet-platelet interactions, and other coagulatory mechanisms.