Multiple snake venom toxins from African elapids and viperids (SVT)

Multiple snake venom toxins from African elapids and viperids represent a complex mixture of bioactive proteins and peptides that serve as the primary drivers of pathology in snakebite envenomation. Elapid venoms, such as those from the Black Mamba (Dendroaspis polylepis) or Forest Cobra (Naja melanoleuca), are characterized by high concentrations of three-finger toxins (3FTxs) and phospholipases A2 (PLA2s) that target the neuromuscular junction, leading to rapid paralysis and respiratory failure (UniProt, 2023). Conversely, viperid venoms from species like the Puff Adder (Bitis arietans) or Saw-scaled Viper (Echis ocellatus) are rich in snake venom metalloproteinases (SVMPs) and serine proteases (SVSPs) that degrade the extracellular matrix and disrupt the coagulation cascade, resulting in local tissue necrosis and systemic hemorrhage (WHO, 2021). These toxins are the primary targets for antivenom therapy, which utilizes purified polyclonal antibodies to bind and neutralize the venom components in the bloodstream. Beyond traditional antivenoms, research is increasingly focused on small-molecule inhibitors like Varespladib and Marimastat, which aim to provide broad-spectrum inhibition of specific enzymatic toxin families to improve outcomes in rural or resource-limited settings (PubMed, 2020).

Other names

African snake venom proteinsElapid and Viperid toxinsOphidian toxinsSnake venom toxins (SVT)

Antivenoms function through the binding of specific IgG or F(ab')2 antibody fragments to venom toxins, neutralizing their biological activity and facilitating their clearance from the systemic circulation. Small molecule inhibitors like Varespladib act as competitive inhibitors of enzymatic toxins such as secreted phospholipase A2 (sPLA2), preventing the hydrolysis of phospholipids and subsequent inflammatory or toxic cascades.