中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis

文献类型:期刊论文

作者Zhang, Lei1,2; Shi, Wanxia1,2; Zeng, Xian-Chun1,2; Ge, Feng3; Yang, Mingkun3; Nie, Yao1,2; Bao, Aorigele1,2; Wu, Shifen1,2; E, Guoji1,2
刊名JOURNAL OF PROTEOMICS
出版日期2015-10-14
卷号128页码:231-250
关键词Scorpion toxin Androctonus bicolor Venom peptide Transcriptomic and proteomic analysis Venom composition Ion channels
ISSN号1874-3919
英文摘要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 1000 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 a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, ICTx-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 a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights 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 channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels. (C) 2015 Elsevier B.V. All rights reserved.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biochemical Research Methods
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]BUTHUS-MARTENSII KARSCH ; ANTI-EPILEPSY PEPTIDE ; MESOBUTHUS-MARTENSII ; MOLECULAR DIVERSITY ; PARABUTHUS-TRANSVAALICUS ; ANTIMICROBIAL PEPTIDES ; TITYUS-SERRULATUS ; CHANNEL TOXIN ; MASS-SPECTROMETRY ; GAINING INSIGHT
收录类别SCI
语种英语
WOS记录号WOS:000364882200021
源URL[http://ir.ihb.ac.cn/handle/342005/27395]  
专题水生生物研究所_水生生物分子与细胞生物学研究中心_期刊论文
作者单位1.China Univ Geosci, Dept Biol Sci & Technol, Sch Environm Studies, Wuhan 430074, Peoples R China
2.China Univ Geosci, State Key Lab Biogeol & Environm Geol, Wuhan 430074, Peoples R China
3.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China
推荐引用方式
GB/T 7714
Zhang, Lei,Shi, Wanxia,Zeng, Xian-Chun,et al. Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis[J]. JOURNAL OF PROTEOMICS,2015,128:231-250.
APA Zhang, Lei.,Shi, Wanxia.,Zeng, Xian-Chun.,Ge, Feng.,Yang, Mingkun.,...&E, Guoji.(2015).Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis.JOURNAL OF PROTEOMICS,128,231-250.
MLA Zhang, Lei,et al."Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis".JOURNAL OF PROTEOMICS 128(2015):231-250.

入库方式: OAI收割

来源:水生生物研究所

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