Snake venom proteins (Bothrops asper and Crotalus durissus)

This entry refers to a diverse group of proteins and peptides derived from the venoms of Bothrops asper (Terciopelo) and Crotalus durissus (South American Rattlesnake). These venoms are complex mixtures containing enzymes such as zinc-dependent metalloproteinases (SVMPs), phospholipases A2 (PLA2s), and serine proteinases (SVSPs), as well as non-enzymatic proteins like disintegrins and C-type lectin-like proteins (UniProt, 2023). While many components are highly toxic, causing hemorrhage, necrosis, and neurotoxicity, specific low-toxicity or non-toxic variants and fragments are of significant interest in pharmacology (PubMed, 2021). For instance, disintegrins from these species are studied for their ability to inhibit platelet aggregation and tumor metastasis by targeting integrin receptors, while certain PLA2 homologs are explored for antimicrobial and anticancer properties (NIH, 2022). Crotamine, a small basic polypeptide from C. durissus, exhibits cell-penetrating properties and selective toxicity toward cancer cells (Toxicon, 2014). In the context of therapeutics, these proteins serve more as drug leads or scaffolds rather than targets themselves, although they are the primary targets for neutralization by polyvalent antivenoms (Gutiérrez et al., 2017).

Other names

Non-toxic or low-toxicity venom proteins from Bothrops asper and Crotalus durissus venomsTerciopelo and Cascabel venom componentsViperid and Crotalid venom proteinsBothrops asper and Crotalus durissus venom proteome

Neutralization by specific antibodies in antivenom; inhibition of enzymatic activity by small molecules like Varespladib; or as therapeutic agents: inhibition of integrin receptors (disintegrins), cleavage of fibrinogen (batroxobin), or inhibition of angiotensin-converting enzyme (BPPs).