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Bitis arietans disintegrins and C-type lectin-like proteins (Snaclecs) are key non-enzymatic components of the Puff Adder venom that potently disrupt the host's hemostatic system (PLOS Neglected Tropical Diseases, 2023). Disintegrins, such as bitistatin (also known as arietin), are small, cysteine-rich peptides that typically utilize an RGD (Arg-Gly-Asp) motif to competitively inhibit the binding of fibrinogen to the platelet integrin alpha-IIb/beta-3, thereby preventing platelet aggregation (UniProt P17497). C-type lectin-like proteins, including the bitiscetin family (bitiscetin-1, -2, and -3), are heterodimeric proteins that interact with von Willebrand factor (VWF) or the platelet glycoprotein Ib (GPIb) receptor (MDPI Toxins, 2022). These interactions lead to either platelet agglutination or the inhibition of VWF-collagen interactions, further compromising blood clotting (Toxicon, 2005). During envenomation, the synergistic action of these proteins results in severe systemic hemorrhage, thrombocytopenia, and coagulopathy, which are the primary clinical manifestations of a Puff Adder bite (NIH, 2023). Consequently, these proteins are the primary targets for neutralization by polyvalent antivenoms in clinical settings (PLOS Neglected Tropical Diseases, 2023). Furthermore, their high affinity and specificity for cardiovascular receptors have made them significant leads in the design of therapeutic antithrombotic agents (ResearchGate, 2022).
Neutralization of venom toxins by polyclonal antibodies to prevent binding to physiological targets such as integrins and von Willebrand factor (NIH, 2023).
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