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The scorpion toxin Bot IX is a potent member of the α‐like family and has a unique N‐terminal sequence extension
Author(s) -
MartinEauclaire MarieFrance,
Salvatierra Juan,
Bosmans Frank,
Bougis Pierre E.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12357
Subject(s) - scorpion venoms , toxin , scorpion toxin , venom , scorpion , biology , amino acid , microbiology and biotechnology , chemistry , biochemistry
We report the detailed chemical, immunological and pharmacological characterization of the α‐toxin Bot IX from the Moroccan scorpion Buthus occitanus tunetanus venom. Bot IX , which consists of 70 amino acids, is a highly atypical toxin. It carries a unique N‐terminal sequence extension and is highly lethal in mice. Voltage clamp recordings on oocytes expressing rat Nav1.2 or insect BgNav1 reveal that, similar to other α‐like toxins, Bot IX inhibits fast inactivation of both variants. Moreover, Bot IX belongs to the same structural/immunological group as the α‐like toxin Bot I. Remarkably, radioiodinated Bot IX competes efficiently with the classical α‐toxin AaH II from Androctonus australis, and displays one of the highest affinities for Nav channels.