Peptidomic and transcriptomic profiling of four distinct spider venoms

PLoS One. 2017 Mar 17;12(3):e0172966. doi: 10.1371/journal.pone.0172966. eCollection 2017.

Abstract

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.

MeSH terms

  • Chromatography, Liquid
  • Peptides / metabolism*
  • Spider Venoms / metabolism*
  • Tandem Mass Spectrometry
  • Transcriptome*

Substances

  • Peptides
  • Spider Venoms

Grants and funding

Swiss Initiative in Systems Biology (Bridge to Industry), SpidX project, (http://www.systemsx.ch/index.php?id=123) funded the project through a grant financially supporting SIB (FL) and University of Bern (LKN, WN) and did not play any role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. Atheris SA and Atheris Laboratories (together Atheris): Authors VO, NH, DK, MA and RS are or were employed by Atheris. Atheris provided support in the form of salaries for authors VO, NH, DK, MA and RS, and research materials, but did not have any additional role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. The specific roles of these authors are articulated in the author contributions section.