Multiple snake venom toxins from African Elapidae and Viperidae species (SVTs)

Multiple snake venom toxins from African Elapidae and Viperidae species represent a complex group of bioactive proteins and peptides that serve as the primary pathological agents in snakebite envenomation across sub-Saharan Africa [1, 3]. The Elapidae family, including cobras (Naja) and mambas (Dendroaspis), primarily produces neurotoxic venoms dominated by three-finger toxins (3FTx) and phospholipases A2 (PLA2) that disrupt neuromuscular transmission, leading to paralysis [2, 4]. Conversely, the Viperidae family, such as carpet vipers (Echis) and puff adders (Bitis), produces venoms rich in snake venom metalloproteinases (SVMPs) and serine proteases (SVSPs) that cause hemorrhage, coagulopathy, and extensive local tissue destruction [3, 4]. These toxins are the primary targets for antivenoms, which utilize purified polyclonal antibodies to neutralize venom components through molecular sequestration [1]. Recent drug development has shifted toward small-molecule inhibitors, such as varespladib for PLA2 and marimastat for SVMPs, which offer potential as heat-stable, broad-spectrum treatments for the early management of envenomation [2, 5]. Understanding the synergistic and redundant nature of these toxins is critical for developing effective pan-African therapeutics to combat this neglected tropical disease.

Other names

African snake venom proteinsElapid and Viperid toxinsSnake venom cocktailSub-Saharan snake venom toxins

Antibody-mediated neutralization of venom components through molecular sequestration; Competitive inhibition of enzymatic toxins such as phospholipases and metalloproteinases.