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Scorpion toxins interact with nicotinic acetylcholine receptors
Author(s) -
Kasheverov Igor E.,
Oparin Peter B.,
Zhmak Maxim N.,
Egorova Natalya S.,
Ivanov Igor A.,
Gigolaev Andrei M.,
Nekrasova Oksana V.,
Serebryakova Marina V.,
Kudryavtsev Denis S.,
Prokopev Nikita A.,
Hoang Anh N.,
Tsetlin Victor I.,
Vassilevski Alexander A.,
Utkin Yuri N.
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13530
Subject(s) - acetylcholine receptor , nicotinic agonist , torpedo , nicotinic acetylcholine receptor , ion channel , chemistry , neurotoxin , acetylcholine , ligand gated ion channel , xenopus , venom , neuromuscular junction , scorpion venoms , scorpion , receptor , biology , biochemistry , pharmacology , neuroscience , gene
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 α‐bungarotoxin binding to both muscle‐type nAChR from Torpedo californica and neuronal human α7 nAChR. Toxins inhibiting nAChRs were identified as OSK‐1 (α‐KTx family) from Orthochirus scrobiculosus and HelaTx1 (κ‐KTx family) from Heterometrus laoticus , both being blockers of voltage‐gated potassium channels. With an IC 50 of 1.6 μ m , 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.