Citation

Zhang L, Shi W, Zeng XC, Ge F, Yang M, Nie Y, Bao A, Wu S, Guoji E. J. Proteomics 2015; 128: 231-250.

Affiliation

Department of Biological Science and Technology, School of Environmental Studies & State Key Laboratory of Biogeology and Environmental Geology, China University of Geosciences (Wuhan), Wuhan 430074, P. R. China.

Copyright

(Copyright © 2015, Elsevier Publishing)

DOI

10.1016/j.jprot.2015.07.030

PMID

26254009

Abstract

Androctonus bicolor is one of the most poisonous scorpion species in the world. However, little has been known about the venom composition of the scorpion. To better understand the molecular diversity and medical significance of the venom from the scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1,000 clones from a cDNA library prepared from the venom glands of the scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to discovery of 103 novel putative venom peptides. These peptides include NaTx-like, KTx-like and CaTx-like peptides, putative antimicrobial peptides, Defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from scorpions. The venom was also analyzed using proteomic technique. The presences of a total of 16 different venom peptides were confirmed by the LC-MS/MS analysis. The discoveries of a wide range of new and new-type venom peptides highlight the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channels-associated diseases and infections caused by antibiotics-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels. BIOLOGICAL SIGNIFICANCES: In this study, we provided integrative view of venom composition of A. bicolor through combined transcriptomic and proteomic approaches. Through transcriptomic analysis, we discovered 103 novel venom peptides from the venom glands of A. bicolor. These peptides include NaTx-like, KTx-like and CaTx-like peptides, putative antimicrobial peptides, Defensin-like peptides, BPP-like peptides, BmKa1-like peptides, Kunitz-type toxins and unique venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bounds, respectively. Using LC-MS/MS, we identified 16 venom peptides from the venom of A. bicolor with high sequence coverage. These data highlight the unique diversity of the venom peptides from the scorpion, and help to better understand the medical significances of the venom. The discovery of the novel venom peptides from the scorpion would provide new templates for the development of therapeutic drugs, and offer molecular probes for the basic researches of various cellular ion channels. To the best of our knowledge, A. bicolor is the first species from the genus Androctonus, of which venomics has been characterized so far.

Language: en