1. Academic Validation
  2. Target switch of centipede toxins for antagonistic switch

Target switch of centipede toxins for antagonistic switch

  • Sci Adv. 2020 Aug 7;6(32):eabb5734. doi: 10.1126/sciadv.abb5734.
Shilong Yang 1 2 Yunfei Wang 2 Lu Wang 3 Peter Kamau 1 4 5 Hao Zhang 1 4 Anna Luo 1 4 Xiancui Lu 1 4 Ren Lai 1 4 5 6 7 8
Affiliations

Affiliations

  • 1 Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences/Key Laboratory of bioactive peptides of Yunnan Province, Kunming Institute of Zoology, Kunming, Yunnan 650223, China.
  • 2 College of Wildlife and Protected Area, Northeast Forestry University, Harbin 150040, China.
  • 3 State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan University, Kunming, Yunnan 650091, China.
  • 4 Kunming College of Life Science, University of Chinese Academy of Sciences, Beijing 100049, China.
  • 5 Sino-African Joint Research Center, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China.
  • 6 KIZ-CUHK Joint Laboratory of Bioresources and Molecular Research in Common Diseases, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China.
  • 7 Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, Hubei 430071, China.
  • 8 Institute for Drug Discovery and Development, Chinese Academy of Sciences, Shanghai 201203, China.
Abstract

Animal Venoms are powerful, highly evolved chemical weapons for defense and predation. While venoms are used mainly to lethally antagonize heterospecifics (individuals of a different species), nonlethal envenomation of conspecifics (individuals of the same species) is occasionally observed. Both the venom and target specifications underlying these two forms of envenomation are still poorly understood. Here, we show a target-switching mechanism in centipede (Scolopendra subspinipes) venom. On the basis of this mechanism, a major toxin component [Ssm Spooky Toxin (SsTx)] in centipede venom inhibits the Shal channel in conspecifics but not in heterospecifics to cause short-term, recoverable, and nonlethal envenomation. This same toxin causes fatal heterospecific envenomation, for example, by switching its target to the Shaker channels in heterospecifics without inhibiting the Shaker channel of conspecific S. subspinipes individuals. These findings suggest that venom components exhibit intricate coevolution with their targets in both heterospecifics and conspecifics, which enables a single toxin to develop graded intraspecific and interspecific antagonistic interactions.

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