Peptidomic and transcriptomic profiling of four distinct spider venoms

Article Article scientifique Article Peptidomic and transcriptomic profiling of four distinct spider venoms eng 2017 author Oldrati Vera Wanda 645841 author Koua Dominique Kadio 646999 author Allard Pierre-Marie 812151 author Hulo Nicolas 29577 author Arrell Miriam author Nentwig Wolfgang author Lisacek Frédérique 0000-0002-0948-4537 639315 author Wolfender Jean-Luc 135649 author Kuhn-Nentwig Lucia author Stocklin Reto 27078 e0172966 10.1371/journal.pone.0172966 28306751 1932-6203 Venom based research is exploited to find novel candidates for the development of innovative pharmacological tools, drug candidates and new ingredients for cosmetic and agrochemical industries. Moreover, venomics, as a well-established approach in systems biology, helps to elucidate the genetic mechanisms of the production of such a great molecular biodiversity. Today the advances made in the proteomics, transcriptomics and bioinformatics fields, favor venomics, allowing the in depth study of complex matrices and the elucidation even of minor compounds present in minute biological samples. The present study illustrates a rapid and efficient method developed for the elucidation of venom composition based on NextGen mRNA sequencing of venom glands and LC-MS/MS venom proteome profiling. The analysis of the comprehensive data obtained was focused on cysteine rich peptide toxins from four spider species originating from phylogenetically distant families for comparison purposes. The studied species were Heteropoda davidbowie (Sparassidae), Poecilotheria formosa (Theraphosidae), Viridasius fasciatus (Viridasiidae) and Latrodectus mactans (Theridiidae). This led to a high resolution profiling of 284 characterized cysteine rich peptides, 111 of which belong to the Inhibitor Cysteine Knot (ICK) structural motif. The analysis of H. davidbowie venom revealed a high richness in term of venom diversity: 95 peptide sequences were identified; out of these, 32 peptides presented the ICK structural motif and could be classified in six distinct families. The profiling of P. formosa venom highlighted the presence of 126 peptide sequences, with 52 ICK toxins belonging to three structural distinct families. V. fasciatus venom was shown to contain 49 peptide sequences, out of which 22 presented the ICK structural motif and were attributed to five families. The venom of L. mactans, until now studied for its large neurotoxins (Latrotoxins), revealed the presence of 14 cysteine rich peptides, out of which five were ICK toxins belonging to the CSTX superfamily. This in depth profiling of distinct ICK peptide families identified across the four spider species highlighted the high conservation of these neurotoxins among spider families. Liquid chromatography Peptides metabolism Spider venoms metabolism Tandem mass spectrometry Transcriptome Dewey 615 Dewey 025.063 13 Centre universitaire d'informatique 0D3 31 Section des sciences pharmaceutiques 17 32 Département d'informatique 18 false 882 Phytochimie et produits naturels bioactifs 1316 Proteome informatics Group PLOS ONE 12 3 fdc5018f-ab93-4013-b970-7b76ed9b9d65 Article (Published version) Public 28306751.pdf 1578279 application/pdf CC BY openAccess Centres et instituts / Centre universitaire d'informatique Faculté des sciences / Section des sciences pharmaceutiques Faculté des sciences / Département d'informatique

Title	Published in	Year	Views	Downloads

Peptidomic and transcriptomic profiling of four distinct spider venoms	PLOS ONE	2017	497	2,250
Venomics to decrypt the biomedical potential of spider toxins		2016	1,136	2

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Oldrati, Vera Wanda