Snake venom toxins from Echis pyramidum (EpV)

Snake venom toxins from Echis pyramidum, the Northeast African carpet viper, comprise a complex mixture of bioactive proteins and peptides that primarily target the circulatory and musculoskeletal systems [Casewell et al., 2014, PubMed]. The most significant components include snake venom metalloproteinases (SVMPs), which degrade the extracellular matrix and basement membranes of blood vessels, leading to systemic hemorrhage [Journal of Venomous Animals and Toxins, 2017]. Additionally, the venom contains potent procoagulants like ecarin, a prothrombin activator that induces venom-induced consumption coagulopathy (VICC) [UniProt P81187]. Phospholipase A2 (PLA2) enzymes within the venom cause local tissue inflammation, pain, and necrosis at the bite site [PubMed: 27464311]. In a clinical context, these toxins are the primary targets for polyvalent antivenoms, which use antibodies to neutralize the venom's enzymatic and toxic activities [WHO Guidelines]. They are also being investigated as targets for small-molecule inhibitors like varespladib and marimastat to provide rapid, field-based treatment for envenomation [Lewin et al., 2016, PubMed]. Understanding the specific proteomic profile of Echis pyramidum is crucial for developing effective therapeutics against the high morbidity and mortality associated with its bite in Northeast Africa [Casewell et al., 2014]. These toxins also serve as valuable tools in hematology research, particularly in assays for blood coagulation factors [UniProt P81187].

Other names

Northeast African carpet viper venomEgyptian saw-scaled viper venomEchis pyramidum venom proteins

Neutralization of enzymatic activity by antibodies; Competitive inhibition of metalloproteinases; Inhibition of phospholipase A2