Binding of an α scorpion toxin to insect sodium channels is not dependent on membrane potential

FEBS Letters

Gordon, Dalia¹  Zlotkin, Eliahu¹ 

[1] The Hebrew University of Jerusalem, Institute of Life Sciences, Department of Cell and Animal Biology, Jerusalem 91904, Israel

关键词: Sodium channel;    Neurotoxin;    Scorpion toxin;    Locusta;    AaIT and AaH II;    an excitatory insect selective toxin and an α mammal toxin;    respectively;    from the venom of the scorpion Androctonus australis;    ATX II;    toxin 2 from the sea anemone Anemonia sulcata;    LqhIT2;    a depressant insect selective toxin from the venom of the scorpion Leiurus quinquestriatus hebraeus;    Ts VII;    a β toxin from the venom of the scorpion Tityus serrulatus;    TTX;    tetrodotoxin.;   

DOI  :  10.1016/0014-5793(93)81147-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The insect-specific LqhαIT toxin resembles α scorpion toxins affecting mammals by its amino acid sequence and effects on sodium conductance. The present study reveals that LqhαIT does not bind to rat brain membranes and possesses in locust neuronal membranes a single class of high affinity (K _d = 1.06 ± 0.15 nM) and low capacity (B _max = 0.7 ± 0.19 protein) binding sites. The latter are: (1) distinct from binding sites of other sodium channel neurotoxins; (2) inhibited by sea anemone toxin II; (3) cooperatively interacting with veratridine; (4) not dependent on membrane potential, in contrast to the binding sites of α toxins in vertebrate systems. These data suggest the occurrence of (a) conformational-structural differences between insect and mammal sodium channels and (b) the animal group specificity and pharmacological importance of the α scorpion toxins.

【 授权许可】

Unknown