African snake venom toxins

African snake venom toxins refer to a complex mixture of bioactive proteins and peptides present in the venom of African snake species, most notably from the Viperidae (e.g., Bitis, Echis) and Elapidae (e.g., Naja, Dendroaspis) families. These venoms contain a variety of enzymes (e.g., phospholipase A2, metalloproteinases, serine proteases), non-enzymatic proteins (e.g., three-finger toxins, C-type lectins), and small polypeptides, each with specific molecular targets and mechanisms[2][4][1][5][6]. Major toxin classes include: \n- Phospholipase A2s, which hydrolyze cell membrane phospholipids and can be neurotoxic, myotoxic, and cytotoxic[5][3];\n- Snake venom metalloproteinases, which destroy tissue integrity and cause hemorrhage[1][4];\n- Three-finger toxins (3FTx), especially in elapid venoms, which bind to neurotransmitter receptors and cause paralysis[6][2];\n- Serine proteases, which affect blood clotting cascades[2]. \nThese toxins act synergistically to immobilize and pre-digest prey, but in humans, cause the spectrum of clinical effects seen in envenomation, including coagulopathy, neurotoxicity, and severe tissue damage. Because “African snake venom toxins” refers to a mixture (>20 classes of molecules[2][4]), not a single defined target, it is not a canonical drug/target receptor or molecule, and thus should not be assigned a canonical Target ID.

Other names

Snake venom toxins (African)African venom proteinsAfrican snake venom components

Phospholipase A2: Hydrolyzes membrane phospholipids, causing cell lysis and inflammation[5][3]; Metalloproteinase: Degrades extracellular matrix, damages vascular endothelium—leading to hemorrhage[4][1]; Three-finger toxins (3FTx): Binds to acetylcholine receptors, blocking neurotransmission (neurotoxicity)[2][6]; C-type lectins: Interfere with blood coagulation by binding clotting factors[6]; L-amino acid oxidase: Generates hydrogen peroxide, causing oxidative stress and cytotoxicity[4]