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Daboia siamensis C-type lectin-like proteins, or snaclecs, are a major class of non-enzymatic toxins found in the venom of the Eastern Russell's viper (Daboia siamensis). These proteins typically exist as disulfide-linked heterodimers that share structural homology with the carbohydrate-recognition domains of C-type lectins but lack the residues necessary for calcium-dependent sugar binding (UniProt, 2024). Instead, they function by binding with high affinity to various blood components, including platelet receptors like glycoprotein Ib (GPIb) and glycoprotein VI (GPVI), as well as coagulation factors such as Factor IX and Factor X (PubMed, 2021). This binding can either induce or inhibit platelet aggregation, contributing significantly to the systemic hemotoxicity, thrombocytopenia, and venom-induced consumption coagulopathy (VICC) observed in snakebite victims (WHO, 2016). In clinical management, these proteins are the primary targets for therapeutic antivenoms, which utilize polyclonal antibodies to neutralize the toxins and restore normal hemostatic function. Beyond their pathological role, they are valuable tools in hematological research for characterizing platelet signaling pathways and developing diagnostic assays for bleeding disorders. Their ability to target specific receptors with high precision also makes them templates for the design of novel anticoagulant and antiplatelet therapeutics (PubChem, 2024).
Neutralization of toxin activity via antibody-mediated binding, preventing interaction with physiological substrates like platelets and coagulation factors.
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