Bot IT2: a new scorpion toxin to study receptor site on insect sodium channels

FEBS Lett. 1997 Mar 17;405(1):77-80. doi: 10.1016/s0014-5793(97)00160-9.

Abstract

The insect-specific Bothus occitanus tunetanus IT2 toxin is distinguishable from other scorpion toxins by its amino acid sequence and effects on sodium conductance. The present study reveals that Bot IT2 possesses in cockroach neuronal membranes a single class of high affinity (Kd = 0.3 +/- 0.1 nM) and low capacity (Bmax = 2.4 +/- 0.5 pmol/mg) binding sites. Competitive binding experiments with several known sodium channel neurotoxins reveal that the Bot IT2 binding site is in close proximity to the other toxins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Membrane / metabolism
  • Neurons / metabolism
  • Neurotoxins / metabolism
  • Periplaneta
  • Scorpion Venoms / chemistry
  • Scorpion Venoms / isolation & purification
  • Scorpion Venoms / metabolism*
  • Sodium Channels / metabolism*

Substances

  • BotIT2 toxin
  • BotIT4 toxin
  • Neurotoxins
  • Scorpion Venoms
  • Sodium Channels
  • scorpion toxin receptor
  • toxin VII
  • scorpion toxin I, Androctonus