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. 2011 Jan 1;170(1):144-55.
doi: 10.1016/j.ygcen.2010.09.018. Epub 2010 Oct 1.

Identification of chelicerate neuropeptides using bioinformatics of publicly accessible expressed sequence tags

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Identification of chelicerate neuropeptides using bioinformatics of publicly accessible expressed sequence tags

Andrew E Christie et al. Gen Comp Endocrinol. .

Abstract

While numerous investigations have focused on the identification of neuropeptides in arthropods, most have been conducted on members of the Hexapoda or Crustacea, and little is currently known about those in the Chelicerata. Here, publicly accessible expressed sequence tags (ESTs) were mined for putative chelicerate neuropeptide-encoding transcripts; the peptides encoded by the ESTs were deduced using on-line peptide prediction programs and homology to known isoforms. Fifty-eight ESTs representing eight peptide families/subfamilies were identified using this strategy. Of note was the prediction of the first authentic chelicerate C-type allatostatin, pQIRYHQCYFNPISCF, from the mite Tetranychus urticae, as well as the prediction a novel allatostatin CC peptide, GEGKMFWRCYFNAVSCF, from both the tick Amblyomma variegatum and the scorpion Mesobuthus gibbosus. Also identified from T. urticae were authentic crustacean cardioactive peptide (CCAP), several peptides belonging to the crustacean hyperglycemic hormone/ion transport peptide superfamily, members of the calcitonin-like diuretic hormone/diuretic hormone 31 family, and several FMRFamide-like peptides, specifically members of the neuropeptide F (NPF) and short neuropeptide F subfamilies. To the best of our knowledge the identifications of CCAP and NPF in T. urticae are the first for the Chelicerata. In addition, several novel orcokinins were identified from the scorpion Scorpiops jendeki and the spider Loxosceles laeta; in S. jendeki previously unknown isoforms of SIFamide, ESRNPPLNGSMFamide and ESKNPPLNGSMFamide, were also predicted. Taken collectively, the data presented in our study expand the catalog of known chelicerate neuropeptides and provide a foundation for future physiological studies of them in these animals.

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