Daboia russelii siamensis C-type lectin-like venom protein (Snaclec)

C-type lectin-like proteins (Snaclecs) from the venom of Daboia russelii siamensis (Eastern Russell's Viper) are non-enzymatic proteins that play a critical role in the pathophysiology of envenomation (PMID: 24530531). These proteins typically exist as heterodimers and exert their effects by binding with high affinity to various components of the hemostatic system, including platelet receptors like Glycoprotein Ib (GPIb) and Glycoprotein VI (GPVI), as well as blood coagulation factors such as Factor X and Factor IX (UniProt: P0C6S0). Depending on their specific structure, they can either induce or inhibit platelet aggregation and interfere with the coagulation cascade, leading to clinical manifestations such as systemic bleeding, consumption coagulopathy, and thrombocytopenia (PMID: 15533511). In a therapeutic context, these proteins are the primary targets for neutralization by monovalent or polyvalent antivenoms, which utilize purified antibodies to sequester the toxins and prevent their binding to physiological targets (WHO Guidelines on Snake Antivenoms). Beyond envenomation, Snaclecs are also studied as molecular tools for understanding vascular biology and as templates for developing novel antithrombotic agents (PMID: 18619475).

Other names

Snake venom C-type lectin-like proteinSnaclecCTLPsRussell's viper C-type lectin

Antivenom-mediated neutralization involves the binding of specific F(ab')2 or IgG antibodies to the toxin's functional sites, preventing the toxin from interacting with host platelet receptors or coagulation factors (PMID: 24530531).