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Daboia siamensis venom C-type lectin-like proteins, commonly referred to as Snaclecs, are a major class of non-enzymatic toxins found in the venom of the Eastern Russell's Viper (Tan et al., 2014, Journal of Proteomics). These proteins typically exist as heterodimers and function by binding with high affinity to various components of the human hemostatic system, including platelet receptors like Glycoprotein Ib and blood coagulation factors such as Factor X and Factor IX (Clemetson, 2010, Toxicon). By interfering with these pathways, they induce or inhibit platelet aggregation and contribute to the severe consumptive coagulopathy and systemic hemorrhage characteristic of Russell's viper envenomation (WHO, 2016, Guidelines for the Management of Snakebites). In a clinical context, these toxins are the primary targets for neutralization by monovalent and polyvalent antivenoms produced by institutions like the Thai Red Cross Society. The interaction between the antivenom antibodies and the Snaclecs prevents the toxins from reaching their physiological targets, thereby halting the progression of venom-induced effects. Furthermore, due to their potent and specific interactions with the vascular system, they serve as valuable tools in hematological research and as templates for the development of novel anticoagulant or antiplatelet therapeutics (UniProt, 2024).
Neutralization of toxin activity through antibody-antigen binding, which prevents the toxin from interacting with physiological targets such as platelet receptors and coagulation factors (WHO, 2016).
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