The scorpion toxin Bot IX is a potent member of the α-like family and has a unique N-terminal sequence extension

5Citations
Citations of this article
11Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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.

Cite

CITATION STYLE

APA

Martin-Eauclaire, M. F., Salvatierra, J., Bosmans, F., & Bougis, P. E. (2016). The scorpion toxin Bot IX is a potent member of the α-like family and has a unique N-terminal sequence extension. FEBS Letters, 590(18), 3221–3232. https://doi.org/10.1002/1873-3468.12357

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free