Genetic mechanisms of scorpion venom peptide diversification.
The diversity of scorpion venom peptides is well shown by the presence of about 400 such polypeptides with or without disulfide bonds. Scorpion toxins with disulfide bonds present a variety of sequence features and pharmacological functions by affecting different ion channels, while the venom peptides without disulfide bonds represent a new subfamily, having much lower sequence homology among each other and different functions (e.g. bradykinin-potentiating, antimicrobial, molecular cell signal initiating and immune modulating). Interestingly, all scorpion venom peptides with divergent functions may have evolved from a common ancestor gene. Over the lengthy evolutionary time, the diversification of scorpion venom peptides evolved through polymorphism, duplication, trans-splicing, or alternative splicing at the gene level. In order to completely clarify the diversity of scorpion toxins and toxin-like peptides, toxinomics (genomics and proteomics of scorpion toxins and toxin-like peptides) are expected to greatly advance in the near future.
Zhijian
Cao
C
State Key Laboratory of Virology, College of Life Sciences, Wuhan Uiniversity, Wuhan 430072, People's Republic of China. zjcao@whu.edu.cn
Feng
Luo
L
Yingliang
Wu
W
Xin
Mao
M
Wenxin
Li
L
D000818:Animals; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D012604:Scorpion Venoms / Q000737:chemistry* / Q000235:genetics; D012605:Scorpions; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D010455:Peptides; D012604:Scorpion Venoms