title: Structural and Functional Diversity of Peptide Toxins from Tarantula Haplopelma hainanum (Ornithoctonus hainana) Venom Revealed by Transcriptomic, Peptidomic, and Patch Clamp Approaches.
abstract: Spider venom is a complex mixture of bioactive peptides to subdue their prey. Early estimates suggested that over 400 venom peptides are produced per species. In order to investigate the mechanisms responsible for this impressive diversity, transcriptomics based on second generation high throughput sequencing was combined with peptidomic assays to characterize the venom of the tarantula Haplopelma hainanum. The genes expressed in the venom glands were identified, and the bioactivity of their protein products was analyzed using the patch clamp technique. A total of 1,136 potential toxin precursors were identified that clustered into 90 toxin groups, of which 72 were novel. The toxin peptides clustered into 20 cysteine scaffolds that included between 4 and 12 cysteines, and 14 of these groups were newly identified in this spider. Highly abundant toxin peptide transcripts were present and resulted from hypermutation and/or fragment insertion/deletion. In combination with variable post-translational modifications, this genetic variability explained how a limited set of genes can generate hundreds of toxin peptides in venom glands. Furthermore, the intraspecies venom variability illustrated the dynamic nature of spider venom and revealed how complex components work together to generate diverse bioactivities that facilitate adaptation to changing environments, types of prey, and milking regimes in captivity.
authors.affiliation: From the Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China and.
authors.forename: Yi-Ya
authors.initials: YY
authors.lastname: Zhang
authors.affiliation: the State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, 20 Dong-Da Street, Fengtai District, Beijing 100071, China.
authors.forename: Yong
authors.initials: Y
authors.lastname: Huang
authors.affiliation: From the Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China and.
authors.forename: Quan-Ze
authors.initials: QZ
authors.lastname: He
authors.affiliation: From the Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China and.
authors.forename: Ji
authors.initials: J
authors.lastname: Luo
authors.affiliation: From the Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China and.
authors.forename: Li
authors.initials: L
authors.lastname: Zhu
authors.affiliation: From the Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China and.
authors.forename: Shan-Shan
authors.initials: SS
authors.lastname: Lu
authors.affiliation: From the Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China and.
authors.forename: Jin-Yan
authors.initials: JY
authors.lastname: Liu
authors.affiliation: From the Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China and.
authors.forename: Peng-Fei
authors.initials: PF
authors.lastname: Huang
authors.affiliation: From the Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China and xiongzhizeng@gmail.com.
authors.forename: Xiong-Zhi
authors.initials: XZ
authors.lastname: Zeng
authors.affiliation: From the Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China and liangsp@hunnu.edu.cn.
authors.forename: Song-Ping
authors.initials: SP
authors.lastname: Liang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003545:Cysteine / Q000737:chemistry; D018076:DNA, Complementary / Q000378:metabolism; D020224:Expressed Sequence Tags; D017353:Gene Deletion; D008969:Molecular Sequence Data; D009154:Mutation; D009474:Neurons / Q000378:metabolism; D009498:Neurotoxins / Q000737:chemistry; D018408:Patch-Clamp Techniques; D010455:Peptides / Q000737:chemistry; D010802:Phylogeny; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*; D051381:Rats; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D013111:Spider Venoms / Q000737:chemistry*; D013112:Spiders; D014158:Transcription, Genetic
chemical_list: D018076:DNA, Complementary; D009498:Neurotoxins; D010455:Peptides; D013111:Spider Venoms; D003545:Cysteine
keywords: 454 sequencing; Haplopelma hainanum; cysteine pattern; ion channel; molecular diversity; molecular evolution; neurotoxin; spider venom; toxin; transcription