The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody

Toxicon. 2003 Mar;41(4):441-9. doi: 10.1016/s0041-0101(02)00360-4.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies / immunology*
  • Antigens / chemistry*
  • Antigens / immunology*
  • Cross Reactions / immunology*
  • Molecular Sequence Data
  • Sequence Alignment
  • Snake Venoms / chemistry*
  • Snake Venoms / immunology*
  • Snakes* / immunology
  • Species Specificity

Substances

  • Antibodies
  • Antigens
  • Snake Venoms