Literature DB >> 15705498

BjalphaIT: a novel scorpion alpha-toxin selective for insects--unique pharmacological tool.

Tal Arnon1, Tamara Potikha, Daniel Sher, Menashe Elazar, Wenfu Mao, Tzachy Tal, Frank Bosmans, Jan Tytgat, Nissim Ben-Arie, Eliahu Zlotkin.   

Abstract

Long-chain neurotoxins derived from the venom of the Buthidae scorpions, which affect voltage-gated sodium channels (VGSCs) can be subdivided according to their toxicity to insects into insect-selective excitatory and depressant toxins (beta-toxins) and the alpha-like toxins which affect both mammals and insects. In the present study by the aid of reverse-phase HPLC column chromatography, RT-PCR, cloning and various toxicity assays, a new insect selective toxin designated as BjalphaIT was isolated from the venom of the Judean Black Scorpion (Buthotus judaicus), and its full primary sequence was determined: MNYLVVICFALLLMTVVESGRDAYIADNLNCAYTCGSNSYCNTECTKNGAVSGYCQWLGKYGNACWCINLPDKVPIRIPGACR (leader sequence is underlined). Despite its lack of toxicity to mammals and potent toxicity to insects, BjalphaIT reveals an amino acid sequence and an inferred spatial arrangement that is characteristic of the well-known scorpion alpha-toxins highly toxic to mammals. BjalphaITs sharp distinction between insects and mammals was also revealed by its effect on sodium conductance of two cloned neuronal VGSCs heterloguously expressed in Xenopus laevis oocytes and assayed with the two-electrode voltage-clamp technique. BjalphaIT completely inhibits the inactivation process of the insect para/tipE VGSC at a concentration of 100 nM, in contrast to the rat brain Na(v)1.2/beta1 which is resistant to the toxin. The above categorical distinction between mammal and insect VGSCs exhibited by BjalphaIT enables its employment in the clarification of the molecular basis of the animal group specificity of scorpion venom derived neurotoxic polypeptides and voltage-gated sodium channels.

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Year:  2005        PMID: 15705498     DOI: 10.1016/j.ibmb.2004.11.005

Source DB:  PubMed          Journal:  Insect Biochem Mol Biol        ISSN: 0965-1748            Impact factor:   4.714


  6 in total

Review 1.  Voltage-gated sodium channel modulation by scorpion alpha-toxins.

Authors:  Frank Bosmans; Jan Tytgat
Journal:  Toxicon       Date:  2006-09-28       Impact factor: 3.033

2.  Molecular analysis of the sea anemone toxin Av3 reveals selectivity to insects and demonstrates the heterogeneity of receptor site-3 on voltage-gated Na+ channels.

Authors:  Yehu Moran; Roy Kahn; Lior Cohen; Maya Gur; Izhar Karbat; Dalia Gordon; Michael Gurevitz
Journal:  Biochem J       Date:  2007-08-15       Impact factor: 3.857

3.  Expression of scorpion toxin LqhIT2 increases the virulence of Metarhizium acridum towards Locusta migratoria manilensis.

Authors:  Guoxiong Peng; Yuxian Xia
Journal:  J Ind Microbiol Biotechnol       Date:  2014-08-29       Impact factor: 3.346

4.  Modular organization of α-toxins from scorpion venom mirrors domain structure of their targets, sodium channels.

Authors:  Anton O Chugunov; Anna D Koromyslova; Antonina A Berkut; Steve Peigneur; Jan Tytgat; Anton A Polyansky; Vladimir M Pentkovsky; Alexander A Vassilevski; Eugene V Grishin; Roman G Efremov
Journal:  J Biol Chem       Date:  2013-05-01       Impact factor: 5.157

5.  The unfulfilled promises of scorpion insectotoxins.

Authors:  Ernesto Ortiz; Lourival D Possani
Journal:  J Venom Anim Toxins Incl Trop Dis       Date:  2015-06-17

6.  Target-Specificity in Scorpions; Comparing Lethality of Scorpion Venoms across Arthropods and Vertebrates.

Authors:  Arie van der Meijden; Bjørn Koch; Tom van der Valk; Leidy J Vargas-Muñoz; Sebastian Estrada-Gómez
Journal:  Toxins (Basel)       Date:  2017-10-04       Impact factor: 4.546

  6 in total

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