Scorpion toxins interact with nicotinic acetylcholine receptors

FEBS Letters

article

Igor E. Kasheverov¹  Peter B. Oparin¹  Maxim N. Zhmak¹  Natalya S. Egorova¹  Igor A. Ivanov¹  Andrei M. Gigolaev¹  Oksana V. Nekrasova¹  Marina V. Serebryakova³  Denis S. Kudryavtsev¹  Nikita A. Prokopev⁴  Anh N. Hoang⁵  Victor I. Tsetlin¹  Alexander A. Vassilevski¹  Yuri N. Utkin¹ 

[1] Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences;Institute of Molecular Medicine, Sechenov First Moscow State Medical University;Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University;Department of Bioorganic Chemistry, Faculty of Biology, Lomonosov Moscow State University;Institute of Applied Materials Science, Vietnam Academy of Science and Technology;Moscow Institute of Physics and Technology (State University)

关键词: neurotoxin;    nicotinic acetylcholine receptor;    potassium channels;    scorpion;    snake;    venom;   

DOI  :  10.1002/1873-3468.13530

来源: John Wiley & Sons Ltd.

【 摘 要 】

Neurotoxins are among the main components of scorpion and snake venoms. Scorpion neurotoxins affect voltage-gated ion channels, while most snake neurotoxins target ligand-gated ion channels, mainly nicotinic acetylcholine receptors (nAChRs). We report that scorpion venoms inhibit a-bungarotoxin binding to both muscle-type nAChR from Torpedo californica and neuronal human a7 nAChR. Toxins inhibiting nAChRs were identified as OSK-1 (aKTx family) from Orthochirus scrobiculosus and HelaTx1 (j-KTx family) from Heterometrus laoticus, both being blockers of voltage-gated potassium channels. With an IC50 of 1.6 lM, OSK1 inhibits acetylcholine-induced current through mouse muscle-type nAChR heterologously expressed in Xenopus oocytes. Other well-characterized scorpion toxins from these families also bind to Torpedo nAChR with micromolar affinities. Our results indicate that scorpion neurotoxins present target promiscuity.

【 授权许可】

Unknown