In silico characterization of the peptidome of the sea louse Caligus rogercresseyi (Crustacea, Copepoda)

Overview
TitleIn silico characterization of the peptidome of the sea louse Caligus rogercresseyi (Crustacea, Copepoda)
AuthorsChristie AE
TypeJournal Article
Journal NameGeneral and comparative endocrinology
Volume204C
IssueN/A
Year2014
Page(s)248-260
CitationChristie AE. In silico characterization of the peptidome of the sea louse Caligus rogercresseyi (Crustacea, Copepoda). General and comparative endocrinology. 2014 Jun 7; 204C:248-260.

Abstract

Copepods of the order Siphonostomatoida are a major concern for commercial aquaculture as many farmed fish serve as hosts for these parasitic crustaceans. Caligus rogercresseyi, a member of the Siphonostomatoida, is a significant problem for salmonid aquaculture in the Southern Hemisphere, and as such, a search for methods for controlling infestations of it is ongoing. One possibility for biological control of this and other copepod ectoparasites is endocrine manipulation. However, little is known about the native endocrine signaling systems in these animals. As part of an ongoing effort to characterize crustacean ectoparasite peptidergic systems, the publicly accessible C. rogercresseyi transcriptome shotgun assembly (TSA) was mined for peptide-encoding transcripts. Using the identified TSA sequences, precursor proteins were deduced and their mature peptides predicted. Thirty-three peptide-encoding transcripts were identified within the Caligus TSA dataset, with the structures of 131 distinct peptides characterized from the deduced pre/preprohormones. The predicted peptides included isoforms of allatostatin A, allatostatin B, bursicon α, bursicon β, corazonin, crustacean cardioactive peptide, crustacean hyperglycemic hormone, diuretic hormone 31, DXXRLamide, FLRFamide, FXGGXamide, GSEFLamide, insulin-like peptide (ILP), intocin, leucokinin, molt-inhibiting hormone, myosuppressin, neuroparsin, neuropeptide F (NPF), orcokinin and tachykinin-related peptide. The predicted ILPs are of particular note as they are the first members of this peptide family identified from a copepod. Similarly, the predicted complement of four distinct NPFs is larger than that known from other crustaceans. Taken collectively, these data greatly expand the known C. rogercresseyi peptidome and provide a foundation for initiating studies of peptidergic control in this species.

Properties
Additional details for this publication include:
Property NameValue
Publication ModelPrint-Electronic
ISSN1095-6840
eISSN1095-6840
Publication Date2014 Jun 7
Journal AbbreviationGen. Comp. Endocrinol.
Elocation10.1016/j.ygcen.2014.05.031
CopyrightCopyright © 2014 Elsevier Inc. All rights reserved.
LanguageEnglish
Language AbbrENG
Publication TypeJournal Article
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PMID: PMID:24914818