Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis
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
2015-10-14
Source PublicationJOURNAL OF PROTEOMICS
ISSN1874-3919
Volume128Pages:231-250
AbstractAndroctonus 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.
SubtypeArticle
KeywordScorpion Toxin Androctonus Bicolor Venom Peptide Transcriptomic And Proteomic Analysis Venom Composition Ion Channels
DOI10.1016/j.jprot.2015.07.030
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Indexed BySCI
Funding OrganizationChina National 973 Research Project, Basic Research and Clinical Application of Venom Peptides from Toxic Animals(2010CB529800) ; China National 973 Research Project, Basic Research and Clinical Application of Venom Peptides from Toxic Animals(2010CB529800) ; Fundamental Research Funds for the Central Universities(CUGL100613 ; Fundamental Research Funds for the Central Universities(CUGL100613 ; CUGL110604 ; CUGL110604 ; CUGL120608) ; CUGL120608) ; China National 973 Research Project, Basic Research and Clinical Application of Venom Peptides from Toxic Animals(2010CB529800) ; China National 973 Research Project, Basic Research and Clinical Application of Venom Peptides from Toxic Animals(2010CB529800) ; Fundamental Research Funds for the Central Universities(CUGL100613 ; Fundamental Research Funds for the Central Universities(CUGL100613 ; CUGL110604 ; CUGL110604 ; CUGL120608) ; CUGL120608)
Language英语
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemical Research Methods
WOS KeywordBUTHUS-MARTENSII KARSCH ; ANTI-EPILEPSY PEPTIDE ; MESOBUTHUS-MARTENSII ; MOLECULAR DIVERSITY ; PARABUTHUS-TRANSVAALICUS ; ANTIMICROBIAL PEPTIDES ; TITYUS-SERRULATUS ; CHANNEL TOXIN ; MASS-SPECTROMETRY ; GAINING INSIGHT
WOS IDWOS:000364882200021
Funding OrganizationChina National 973 Research Project, Basic Research and Clinical Application of Venom Peptides from Toxic Animals(2010CB529800) ; China National 973 Research Project, Basic Research and Clinical Application of Venom Peptides from Toxic Animals(2010CB529800) ; Fundamental Research Funds for the Central Universities(CUGL100613 ; Fundamental Research Funds for the Central Universities(CUGL100613 ; CUGL110604 ; CUGL110604 ; CUGL120608) ; CUGL120608) ; China National 973 Research Project, Basic Research and Clinical Application of Venom Peptides from Toxic Animals(2010CB529800) ; China National 973 Research Project, Basic Research and Clinical Application of Venom Peptides from Toxic Animals(2010CB529800) ; Fundamental Research Funds for the Central Universities(CUGL100613 ; Fundamental Research Funds for the Central Universities(CUGL100613 ; CUGL110604 ; CUGL110604 ; CUGL120608) ; CUGL120608)
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Cited Times:24[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/27395
Collection藻类生物学及应用研究中心_水生生物分子与细胞生物学研究中心
Affiliation1.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
Recommended Citation
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.
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