期刊论文详细信息
FEBS Letters
δ‐Atracotoxins from Australian funnel‐web spiders compete with scorpion α‐toxin binding on both rat brain and insect sodium channels
Gordon, Dalia2  Little, Michelle J1  Nicholson, Graham M1  Cestèle, Sandrine3  Wilson, Harry1  Martin-Eauclaire, Marie-France3  Tyler, Margaret I4  Zappia, Cathy1 
[1] Department of Health Sciences, University of Technology, Sydney, Broadway, N.S.W. 2007, Australia;CEA, C.E.-Saclay, Département d'Ingénierie et d'Études des Protéines, Gif-sur-Yvette, F-91911, France;UNRS 6560 CNRS, Laboratoire de Biochimie, Université de la Mediterranée, I.F.R. Jean Roche, 13916 Marseille Cedex 20, France;Deakin Research Ltd., CSIRO Division of Food Processing, North Ryde, N.S.W. 2113, Australia
关键词: Funnel-web spider toxin;    δ-Atracotoxin;    Sodium channel;    Scorpion toxin;    Rat brain synaptosome;    Cockroach neuronal membrane;    δ-Atracotoxin-Ar1 (formerly robustoxin) from Atrax robustus;    δ-Atracotoxin-Hv1 (formerly versutoxin) from Hadronyche versuta;    AaH II;    α-toxin from the venom of the scorpion Androctonus australis hector;    LqhαIT;    α-toxin highly active on insects from the venom of the scorpion Leiurus quinquestriatus hebraeus;    TFA;    trifluoroacetic acid;    RP-HPLC;    reverse phase high performance liquid chromatography;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;    HEPES;    N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid;    Tris;    2-amino-2-(hydroxymethyl) propane-1;    3-diol;    [3H]STX;    [3H]saxitoxin;    [3H]BTX;    [3H]batrachotoxinin A-20α-benzoate;    BSA;    bovine serum albumin;    AaIT;    excitatory insect-selective toxin from the venom of the scorpion Androctonus australis hector;   
DOI  :  10.1016/S0014-5793(98)01378-7
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

δ-Atracotoxins are novel peptide toxins from the venom of Australian funnel-web spiders that slow sodium current inactivation in a similar manner to scorpion α-toxins. To analyse their interaction with known sodium channel neurotoxin receptor sites we determined their effect on scorpion toxin, batrachotoxin and saxitoxin binding. Nanomolar concentrations of δ-atracotoxin-Hv1 and δ-atracotoxin-Ar1 completely inhibited the binding of the scorpion α-toxin AaH II to rat brain synaptosomes as well as the binding of LqhαIT, a scorpion α-toxin highly active on insects, to cockroach neuronal membranes. Moreover, δ-atracotoxin-Hv1 cooperatively enhanced batrachotoxin binding to rat brain synaptosomes in an analogous fashion to scorpion α-toxins. Thus the δ-atracotoxins represent a new class of toxins which bind to both mammalian and insect sodium channels at sites similar to, or partially overlapping with, the receptor binding sites of scorpion α-toxins.

【 授权许可】

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