Identification of Lectins in Snake Venoms

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Abstract
Venoms from 17 spp. [Agkistrodon contortrix contortrix, Agkistrodon rhodostoma, Agkistrodon piscivorus leucostoma, Ancistrodon piscivorus piscivorus, Bothrops atrox, Crotalus adamanteus, Crotalus atrox, Crotalus scutulantus, Lachesis muta, Trimeresurus flavoviridis, Bitis arietans, Causus rhombeatus, Vipera russelli, Bungarus fasciatus, Dendroaspis jamesonii, Naja haje annulifera, Ophiophagus hannah] of snakes representing the families Crotalidae, Elapidae and Viperidae were screened for hemagglutination activity. All venoms, with the exception of venom from Bitis arietans, contained an agglutinin which cross-linked trypsin-treated, formaldehyde-fixed erythrocytes. Venom agglutinins from snakes within the same family demonstrated similarities with regard to ligand specificity, requirements for divalent cations and sensitivity to reducing agent. There were few similarities detected for venom agglutinins from snakes belonging to different families. Venoms from the family Crotalidae contained Ca-dependent lectins blockable by lactose and sensitive to reducing agent. The only crotalid venom agglutinin insensitive to reducing agent was found in the venom of L. muta. Elapid venom agglutinins were Ca-independent and insensitive to reducing agent. The activity of only 1 of these agglutinins was blockable by lactose. The other 3 elapid agglutinins were inhibited by heparin. Agglutination activity was weak and variable or non-existent in venoms from snakes in the family Viperidae.