The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody.
We have demonstrated previously that antisera from mice immunised with DNA encoding the carboxy-terminal domain (JD9) of a potent haemorrhagic metalloproteinase, jararhagin, neutralised over 70% of the haemorrhagic activity of the whole Bothrops jararaca venom. Here, we demonstrate that the JD9-specific antibody possesses extensive immunological reactivity to venom components in snakes of distinct species and genera. The polyspecific immunological reactivity of the antibody showed a correlation with amino acid sequence identity and with predicted antigenic domains of JD9-analogues in venoms of snakes with closest phylogenetic links to B. jararaca. This study further promotes the potential of DNA immunisation to generate toxin-specific antibodies with polyspecific cover. An analysis of the reactivity of the JD9-specific antisera to B. atrox complex venoms that exhibited intraspecific variation in the venom proteome revealed, however, that the toxin-specific approach to antivenom development requires a more in-depth knowledge of the target molecules than is required for conventional antivenoms.
Harrison
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Alistair Reid Venom Research Unit, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool L3 5QA, UK. robharr@liverpool.ac.uk
Wüster
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Theakston
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D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000276:immunology*; D000941:Antigens / Q000737:chemistry* / Q000276:immunology*; D003429:Cross Reactions / Q000276:immunology*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D012910:Snake Venoms / Q000737:chemistry* / Q000276:immunology*; D012911:Snakes / Q000276:immunology; D013045:Species Specificity
D000906:Antibodies; D000941:Antigens; D012910:Snake Venoms