Snake venom C-type lectin-like protein (Snaclec)

Snake venom C-type lectin-like proteins (snaclecs) are a major family of non-enzymatic toxins found primarily in the venom of vipers and pit vipers (Clemetson, 2010, Toxicon). Structurally, they belong to the C-type lectin domain superfamily but generally lack the functional calcium-binding residues necessary for carbohydrate recognition, instead evolving to bind protein targets with high specificity (Morita, 2005, Toxicon). These proteins disrupt host hemostasis by binding to platelet receptors such as Glycoprotein Ib (GPIb), Glycoprotein VI (GPVI), and C-type lectin-like receptor 2 (CLEC-2), or to blood coagulation factors like Factor IX and Factor X (Lu et al., 2005, J Thromb Haemost). Such interactions can either induce or inhibit platelet aggregation and the coagulation cascade, leading to clinical complications like venom-induced consumptive coagulopathy and systemic hemorrhage (Eble, 2019, Molecules). In a therapeutic context, snaclecs are the primary targets for neutralization by antivenoms, which consist of antibodies that bind the toxins and prevent their interaction with host proteins. Furthermore, due to their high affinity for vascular receptors, snaclecs serve as valuable research tools and structural templates for the development of novel anticoagulant and antiplatelet drugs (Clemetson, 2010, Toxicon).

Other names

C-type lectin-like proteinsSV-CTLPsSnake venom lectin-related proteinsSnaclecs

Antivenom antibodies bind to the snaclec proteins, preventing their interaction with host platelet receptors and coagulation factors, thereby neutralizing their toxic effects on the hemostatic system.