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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

(2016) FEBS LETTERS. 590(18). p.3221-3232
Author
Organization
Abstract
We report the detailed chemical, immunological and pharmacological characterization of the -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 -like toxins, Bot IX inhibits fast inactivation of both variants. Moreover, Bot IX belongs to the same structural/immunological group as the -like toxin Bot I. Remarkably, radioiodinated Bot IX competes efficiently with the classical -toxin AaH II from Androctonus australis, and displays one of the highest affinities for Nav channels.
Keywords
Nav channel, scorpion toxin, alpha-like toxin, ANDROCTONUS-AUSTRALIS-HECTOR, MAMMALIAN SODIUM-CHANNELS, SEA-ANEMONE TOXIN, MOLECULAR-BASIS, VOLTAGE-SENSOR, RAT-BRAIN, BMK M1, FUNCTIONAL SITE, RECEPTOR-SITES

Citation

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Chicago
Martin-Eauclaire, Marie-France, Juan Salvatierra, Pascal Mansuelle, Frank Bosmans, and Pierre E Bougis. 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.
APA
Martin-Eauclaire, M.-F., Salvatierra, J., Mansuelle, P., 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.
Vancouver
1.
Martin-Eauclaire M-F, Salvatierra J, Mansuelle P, Bosmans F, Bougis PE. The scorpion toxin Bot IX is a potent member of the α-like family and has a unique N-terminal sequence extension. FEBS LETTERS. 2016;590(18):3221–32.
MLA
Martin-Eauclaire, Marie-France, Juan Salvatierra, Pascal Mansuelle, et al. “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 (2016): 3221–3232. Print.
@article{8584495,
  abstract     = {We report the detailed chemical, immunological and pharmacological characterization of the -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 -like toxins, Bot IX inhibits fast inactivation of both variants. Moreover, Bot IX belongs to the same structural/immunological group as the -like toxin Bot I. Remarkably, radioiodinated Bot IX competes efficiently with the classical -toxin AaH II from Androctonus australis, and displays one of the highest affinities for Nav channels.},
  author       = {Martin-Eauclaire, Marie-France and Salvatierra, Juan and Mansuelle, Pascal and Bosmans, Frank and Bougis, Pierre E},
  issn         = {0014-5793},
  journal      = {FEBS LETTERS},
  language     = {eng},
  number       = {18},
  pages        = {3221--3232},
  title        = {The scorpion toxin Bot IX is a potent member of the \ensuremath{\alpha}-like family and has a unique N-terminal sequence extension},
  url          = {http://dx.doi.org/10.1002/1873-3468.13185},
  volume       = {590},
  year         = {2016},
}

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