A molluscivorous Conus toxin: conserved frameworks in conotoxins

Biochemistry. 1989 Jan 10;28(1):358-61. doi: 10.1021/bi00427a049.

Abstract

We purified and characterized a 27 amino acid toxin from a snail-hunting Conus venom, Conus textile. This toxin causes convulsive-like activity in snails and causes subordinate lobsters to assume an exaggerated dominant posture. The sequence of this peptide is Trp-Cys-Lys-Gln-Ser-Gly-Glu-Met-Cys-Asn-Leu-Leu-Asp-Gln-Asn-Cys-Cys-Asp- Gly-Tyr-Cys-Ile-Val-Leu-Val-Cys-Thr. The sequence was confirmed by determining the nucleotide sequence of a cDNA clone coding for the peptide. The conservation of Cys residues compared to the omega-conotoxins from piscivorous Conus venom suggests that toxins from different cone venoms may use only a few "Cys-motifs" as conserved structural backbones for targeting to a variety of receptors in different animals.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Conotoxins*
  • Cysteine
  • DNA / genetics
  • Molecular Sequence Data
  • Mollusk Venoms* / genetics
  • Mollusk Venoms* / isolation & purification
  • Snails / analysis
  • Snails / genetics

Substances

  • Conotoxins
  • Conus textile toxin
  • Mollusk Venoms
  • DNA
  • Cysteine