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Proc Natl Acad Sci U S A. 2018 Feb 13;115(7):1646-1651. doi: 10.1073/pnas.1714760115. Epub 2018 Jan 22.

Centipedes subdue giant prey by blocking KCNQ channels.

Luo L1,2,3, Li B1,2,3, Wang S4, Wu F5,6, Wang X7,8, Liang P7,8, Ombati R1,2,3, Chen J9, Lu X1,2,3, Cui J10,11, Lu Q1,2, Zhang L5,6, Zhou M12,13, Tian C14,6, Yang S15,2, Lai R15,2.

Author information

1
Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Kunming 650223, Yunnan, China.
2
Key Laboratory of Bioactive Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming 650223, Yunnan, China.
3
University of Chinese Academy of Sciences, Beijing 100049, China.
4
Key Laboratory of Molecular Biophysics of the Ministry of Education College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei 430074, China.
5
Hefei National Laboratory of Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China.
6
High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230027, China.
7
The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310006, China.
8
Institute of Translational Medicine, Zhejiang University, Hangzhou 310058, China.
9
Chongzhou People's Hospital, Sichuan Academy of Medical Sciences, Chengdu 611230, China.
10
Ion Channel Research and Drug Development Center, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China.
11
Department of Biomedical Engineering, Center for the Investigation of Membrane Excitability Diseases, Washington University in St Louis, St. Louis, MO 63130.
12
Ion Channel Research and Drug Development Center, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China; mzhou@bcm.edu cltian@ustc.edu.cn yangsl@mail.kiz.ac.cn rlai@mail.kiz.ac.cn.
13
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030.
14
Hefei National Laboratory of Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China; mzhou@bcm.edu cltian@ustc.edu.cn yangsl@mail.kiz.ac.cn rlai@mail.kiz.ac.cn.
15
Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Kunming 650223, Yunnan, China; mzhou@bcm.edu cltian@ustc.edu.cn yangsl@mail.kiz.ac.cn rlai@mail.kiz.ac.cn.

Abstract

Centipedes can subdue giant prey by using venom, which is metabolically expensive to synthesize and thus used frugally through efficiently disrupting essential physiological systems. Here, we show that a centipede (Scolopendra subspinipes mutilans, ∼3 g) can subdue a mouse (∼45 g) within 30 seconds. We found that this observation is largely due to a peptide toxin in the venom, SsTx, and further established that SsTx blocks KCNQ potassium channels to exert the lethal toxicity. We also demonstrated that a KCNQ opener, retigabine, neutralizes the toxicity of a centipede's venom. The study indicates that centipedes' venom has evolved to simultaneously disrupt cardiovascular, respiratory, muscular, and nervous systems by targeting the broadly distributed KCNQ channels, thus providing a therapeutic strategy for centipede envenomation.

KEYWORDS:

KCNQ; SsTx; centipede; toxicity

PMID:
29358396
PMCID:
PMC5816164
DOI:
10.1073/pnas.1714760115
[Indexed for MEDLINE]
Free PMC Article

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