Cloning of a prothrombin activator-like metalloproteinase from the West African saw-scaled viper, Echis ocellatus.
Systemic envenoming by the saw-scaled viper, Echis ocellatus, is responsible for more deaths than any other snake in West Africa. Despite its medical importance, there have been few investigations into the toxin composition of the venom of this viper. Here we describe the isolation of E. ocellatus venom gland cDNAs encoding a protein of 514 amino acids that showed 91% sequence similarity to Ecarin, a prothrombin-activating metalloproteinase from the venom of the East African viper, E. pyramidum leakeyi, that induces severe consumption coagulopathy. Structural similarities between the E. ocellatus metalloproteinase and analogues in venoms of related vipers suggest that antibodies raised to phylogenetically conserved E. ocellatus metalloproteinase domains may have potential for cross-specific and cross-generic neutralisation of analogous venom toxins.
Alistair Reid Venom Research Unit, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool L3 5QA, UK.
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Hasson
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Theakston
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Harrison
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics*; D004789:Enzyme Activation / Q000235:genetics*; D045726:Metalloproteases / Q000235:genetics*; D008969:Molecular Sequence Data; D011516:Prothrombin / Q000378:metabolism; D016415:Sequence Alignment; D017385:Sequence Homology; D014757:Viper Venoms / Q000235:genetics*; D017819:Viperidae / Q000235:genetics*
D018076:DNA, Complementary; D014757:Viper Venoms; D011516:Prothrombin; D045726:Metalloproteases