Specificity of antibodies to sea anemone toxin III and immunogenicity of the pharmacological site of anemone and scorpion toxins

Eur J Biochem. 1989 Mar 1;180(1):55-60. doi: 10.1111/j.1432-1033.1989.tb14614.x.

Abstract

Toxin III (ATX III) of the sea anemone (Anemonia sulcata) is a polypeptide containing 27 amino acid residues. It has no sequence similarity with other toxins (ATX I and II) from the same species, or with scorpion toxins, although they apparently act in a similar manner by prolonging action potentials. The specificity of ATX III antibodies was characterized using ATX III, ATX I, native and chemically modified ATX II, and scorpion alpha-toxins. The results obtained suggest that a region of ATX III, partially or totally overlapping the pharmacological site shared with ATX I and ATX II, is immunogenic. It includes a guanidino and at least two carboxylate groups. The corresponding region is not immunogenic in ATX I and ATX II. Anti-(ATX III) antibodies recognize the similar regions of ATX I and ATX II and apparently do not recognize scorpion toxins.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Action Potentials / drug effects
  • Animals
  • Antibody Specificity*
  • Antigen-Antibody Reactions*
  • Binding Sites, Antibody
  • Cnidaria / immunology*
  • Cnidarian Venoms / immunology*
  • Cnidarian Venoms / pharmacology
  • Cross Reactions
  • Epitopes
  • Immune Sera / analysis
  • Immunoglobulin G / isolation & purification
  • Neutralization Tests
  • Radioimmunoassay
  • Scorpion Venoms / immunology*
  • Scorpion Venoms / pharmacology
  • Sea Anemones / immunology*

Substances

  • Cnidarian Venoms
  • Epitopes
  • Immune Sera
  • Immunoglobulin G
  • Scorpion Venoms
  • toxin II (Anemonia sulcata)
  • toxin III (Anemonia sulcata)