Structural and Functional Diversity of Peptide Toxins from Tarantula Haplopelma hainanum (Ornithoctonus hainana) Venom Revealed by Transcriptomic, Peptidomic, and Patch Clamp Approaches.

The Journal of Biological Chemistry
Yi-Ya ZhangSong-Ping Liang

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 rev...Continue Reading

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Citations

May 13, 2015·Toxicon : Official Journal of the International Society on Toxinology·Fan ZhangZhonghua Liu
Jul 28, 2016·Toxins·Andreas Hougaard LaustsenMikael Engmark
Aug 21, 2016·Integrative and Comparative Biology·Ricardo C Rodríguez de la Vega, Tatiana Giraud
Oct 28, 2016·Molecular BioSystems·Vera OldratiReto Stöcklin
Jan 17, 2020·PeerJ·Zhili DengYiya Zhang
Jul 28, 2021·Comparative Biochemistry and Physiology. Part D, Genomics & Proteomics·Qianqian HanZewen Liu

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