Citation

Yang S, Liu Z, Xiao Y, Li Y, Rong M, Liang S, Zhang Z, Yu H, King GF, Lai R. Mol. Cell Proteomics 2012; 11(9): 640-650.

Affiliation

Chinese Academy of Sciences, China;

Copyright

(Copyright © 2012, American Society for Biochemistry and Molecular Biology)

DOI

10.1074/mcp.M112.018853

PMID

22595790

Abstract

Centipedes are excellent predatory arthropods that inject venoms to kill or immobilize their prey. Although centipedes have long been known to be venomous, their venoms remain largely unexplored. The chemical components responsible for centipede predation and the functional mechanisms are unknown. Twenty-six neurotoxin-like peptides belonging to ten groups were identified from the centipede venoms, Scolopendra subspinipes mutilans L. Koch by peptidomics combined with transcriptome analysis, revealing the extreme diversity of neurotoxins. These neurotoxins each contain 2-4 intra-molecular disulfide bridges, and in most cases the disulfide framework is different to that found in neurotoxins from the venoms of spiders, scorpions, marine cone snails, sea anemones, and snakes (5S animals). Several neurotoxins contain potential insecticidal abilities and they are found to act on voltage-gated sodium, potassium, and calcium channels, respectively. Although these neurotoxins are functionally similar to the disulfide-rich neurotoxins found in the venoms of 5S animals in that they modulate the activity of voltage-gated ion channels, in almost all cases the primary structures of the centipede-venom peptides are unique. This represents an interesting case of convergent evolution in which different venomous animals have evolved different molecular strategies for targeting the same ion channels in prey and predators. Moreover, the high level of biochemical diversity revealed in this study suggests that centipede venoms might be attractive subjects for prospecting and screening for peptide candidates with potential pharmaceutical or agrochemical applications.

Language: en