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A Novel Toxin from Haplopelma lividum Selectively Inhibits the NaV1.8 Channel and Possesses Potent Analgesic Efficacy

7,* , 1,2,3,* and 1,2,3,*
Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences & Yunnan Province, Kunming Institute of Zoology, Kunming 650223, Yunnan, China
United Laboratory of Natural Peptide of University of Science and Technology of China & Kunming Institute of Zoology, Chinese Academy of Science, Kunming 650223, Yunnan, China
Sino-African Joint Research Center, Chinese Academy of Science, Wuhan 430074, Hubei, China
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense 5230, Denmark
The Danish Diabetes Academy, Odense 5230, Denmark
Life Sciences College, Nanjing Agricultural University, Nanjing 210095, Jiangsu, China
Key Laboratory of Animal Physiology, Biochemistry and Molecular Biology of Hebei Province, College of Life Sciences, Hebei Normal University, Shijiazhuang 050024, Hebei, China
These authors contributed equally to this work.
Authors to whom correspondence should be addressed.
Academic Editor: Richard J. Lewis
Received: 15 October 2016 / Revised: 16 December 2016 / Accepted: 19 December 2016 / Published: 26 December 2016
(This article belongs to the Section Animal Venoms)
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Spider venoms are a complex mixture of peptides with a large number of neurotoxins targeting ion channels. Although thousands of peptide toxins have been identified from venoms of numerous species of spiders, many unknown species urgently need to be investigated. In this study, a novel sodium channel inhibitor, µ-TRTX-Hl1a, was identified from the venom of Haplopelma lividum. It contained eight cysteines and formed a conserved cysteine pattern of ICK motif. µ-TRTX-Hl1a inhibited the TTX-resistant (TTX-r) sodium channel current rather than the TTX-sensitive (TTX-s) sodium channel current. Meanwhile, µ-TRTX-Hl1a selectively inhibited NaV1.8 with an IC50 value of 2.19 μM. Intraperitoneal injection of µ-TRTX-Hl1a dose-dependently reduced inflammatory and neuropathic pain in rodent models of formalin-induced paw licking, tail-flicking, acetic acid-induced writhing, and hot plate test. It showed a better analgesic effect than morphine in inflammatory pain and equipotent effect to morphine in neuropathic pain. These findings demonstrate that µ-TRTX-Hl1a might be a valuable tool for physiology studies on NaV1.8 and a promising lead molecule for pain therapeutics. View Full-Text
Keywords: spider; venom; neurotoxin; NaV1.8; analgesia spider; venom; neurotoxin; NaV1.8; analgesia

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Meng, P.; Huang, H.; Wang, G.; Yang, S.; Lu, Q.; Liu, J.; Lai, R.; Rong, M. A Novel Toxin from Haplopelma lividum Selectively Inhibits the NaV1.8 Channel and Possesses Potent Analgesic Efficacy. Toxins 2017, 9, 7.

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