Venom toxin-specific antibodies offer a more rational treatment of snake envenoming than conventional antivenom. Here, we describe novel cDNAs encoding phospholipase A2 (PLA2) isoforms from venom gland RNA of Echis pyramidum leakeyi (Epl), Echis sochureki (Es) and Echis ocellatus (Eo). The deduced amino acid sequences of these cDNAs encoded proteins with high overall sequence identity to the viper group II PLA2 protein family, including the 14 cysteine residues capable of forming seven disulphide bonds that characterize this group of PLA2 enzymes. Comparison of the PLA2 sequences from Echis with those from related vipers failed to make significant geographic, taxonomic or PLA2-function distinctions between these Echis PLA2 isoforms. However, their deduced hydrophilicity profiles revealed a conserved tertiary structure that we will exploit, by epidermal DNA immunization, to generate PLA2- neutralizing antibodies with polyspecific potential.
ASJC Scopus subject areas