title: Genetic mechanisms of scorpion venom peptide diversification.
abstract: 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.
authors.affiliation: State Key Laboratory of Virology, College of Life Sciences, Wuhan Uiniversity, Wuhan 430072, People's Republic of China. zjcao@whu.edu.cn
authors.forename: Cao
authors.initials: C
authors.lastname: Zhijian
authors.forename: Luo
authors.initials: L
authors.lastname: Feng
authors.forename: Wu
authors.initials: W
authors.lastname: Yingliang
authors.forename: Mao
authors.initials: M
authors.lastname: Xin
authors.forename: Li
authors.initials: L
authors.lastname: Wenxin
mesh_terms: 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
chemical_list: D010455:Peptides; D012604:Scorpion Venoms