Echis ocellatus C-type lectin-like protein (EoCTL)

Echis ocellatus C-type lectin-like proteins, often referred to as snaclecs, are major non-enzymatic components of the venom of the West African Carpet Viper, one of the most medically significant snakes in sub-Saharan Africa [1]. These proteins typically form disulfide-linked heterodimers that lack the calcium-binding properties of classical C-type lectins, instead evolving to bind with high affinity to various host physiological targets [2]. Their primary biological function involves the disruption of hemostasis by binding to platelet receptors such as Glycoprotein Ib (GPIb) or Glycoprotein VI (GPVI), and blood coagulation factors like Factor IX and Factor X [3]. This interaction leads to either the induction or inhibition of platelet aggregation, contributing to the severe systemic hemorrhage and venom-induced consumptive coagulopathy (VICC) observed in snakebite victims [4]. In a therapeutic context, these proteins are the primary targets for neutralization by antivenoms, such as EchiTAbG and Antivipmyn, which employ purified antibodies to sequester the toxins and prevent their pathological effects [5]. Beyond their role in envenomation, these proteins serve as valuable templates for the design of novel anticoagulant and antiplatelet pharmacological agents due to their high specificity for blood components [6]. Citations: [1] UniProt Taxonomy: Echis ocellatus (8701); [2] Clemetson, K. J. (2010). Toxicon; [3] Morita, T. (2005). Journal of Thrombosis and Haemostasis; [4] Casewell, N. R., et al. (2010). BMC Genomics; [5] Harrison, R. A., et al. (2009). PLoS Neglected Tropical Diseases; [6] PubMed: Snake venom proteins as drug leads.

Other names

SnaclecEchis ocellatus lectin-like proteinC-type lectin-like venom proteinCLPWest African Carpet Viper C-type lectin

Neutralization of toxin activity through antibody binding, preventing the interaction between the venom proteins and host targets such as platelet receptors and coagulation factors [5].