Characterization of the Venom Proteome for the Wandering Spider, Ctenus hibernalis (Aranea: Ctenidae)

Abstract

Spider venom is a rich multicomponent mixture of neurotoxic polypeptides. The venom of a small percentage of the currently classified spiders has been categorized. In order to determine what venom proteins are expressed in our species, the wandering spider Ctenus hibernalis, we constructed a comprehensive proteome derived from a crude venom extract using a GeLC approach that required a one dimensional denatured gel electrophoresis separation combined with enzymatic digestion of the entire lane cut into many molecular weight fractions followed by LC-ESI-MS2. In this way, we identified 1,182 proteins with >99% confidence that closely matched sequences derived from the combined genomes taken from several similar species of spiders. Our results suggest that the venom proteins of C. hibernalis contain several proteins with conserved sequences similar to other species. Going forward, with next generation sequencing (NSG), combined with extended annotations will be used to construct a more complete genoproteomic database. Therefore, it is expected that with further studies like this, there will be a continued and growing understand of the genoproteomic makeup of the venom for many species derived from insects, plants, and animals. We believe that as a whole these approaches will lead to a much better understanding of the biology behind venoms of all types, as well as ways to treat exposed patients while also expanding upon and taking advantage of the various positive sides of venomous toxins.Citation: Cole J, Buszka PA, Mobley JA, Hataway RA (2016) Characterization of the Venom Proteome for the Wandering Spider, Ctenus hibernalis (Aranea: Ctenidae).

Composition and toxicity of venom produced by araneophagous white-tailed spiders (Lamponidae: Lampona sp.)

“…It is possible that toxins with a more complex structure than the typical ICK motif, and containing more than six cysteine residues, are prominent in the Araneomorphae infraorder, although such a conclusion may be premature based on the current limited sampling of araneomorph spider venoms 24 . Indeed, these two lampotoxin families show complex cysteine scaffolds, similar to other toxins reported to exist in araneomorph venoms [24][25][26][27][28][29] . Cysteine-rich venom peptides are typically neurotoxins that target various ion channels 30 , suggesting a similar role for these Lampona peptides.…”

“…to obtain two separate venom gland transcriptomes. Transcriptome assembly was performed using Trinity 61 in three runs with different kmer setting (21,25,31) to optimise the results as advised by the Trinity authors. All standalone assemblies were combined and clustered based on nucleotide/amino-acid sequence similarity using the EvidentialGene toolset 62 .…”