Characterisation of proteins in excretory/secretory products collected from salmon lice, Lepeophtheirus salmonis

Overview
TitleCharacterisation of proteins in excretory/secretory products collected from salmon lice, Lepeophtheirus salmonis
AuthorsHamilton S, McLean K, Monaghan SJ, McNair C, Inglis NF, McDonald H, Adams S, Richards R, Roy W, Smith P, Bron J, Nisbet AJ, Knox D
TypeJournal Article
Journal NameParasites & vectors
Volume11
Issue1
Year2018
Page(s)294
CitationHamilton S, McLean K, Monaghan SJ, McNair C, Inglis NF, McDonald H, Adams S, Richards R, Roy W, Smith P, Bron J, Nisbet AJ, Knox D. Characterisation of proteins in excretory/secretory products collected from salmon lice, Lepeophtheirus salmonis. Parasites & vectors. 2018 May 11; 11(1):294.

Abstract

BACKGROUND
The salmon louse, Lepeophtheirus salmonis, is an ectoparasitic copepod which feeds on the mucus, skin and blood of salmonid fish species. The parasite can persist on the surface of the fish without any effective control being exerted by the host immune system. Other ectoparasitic invertebrates produce compounds in their saliva, excretions and/or secretions which modulate the host immune responses allowing them to remain on or in the host during development. Similarly, compounds are produced in secretions of L. salmonis which are thought to be responsible for immunomodulation of the host responses as well as other aspects of crucial host-parasite interactions.

METHODS
In this study we have identified and characterised the proteins in the excretory/secretory (E/S) products of L. salmonis using LC-ESI-MS/MS.

RESULTS
In total 187 individual proteins were identified in the E/S collected from adult lice and pre-adult sea lice. Fifty-three proteins, including 13 serine-type endopeptidases, 1 peroxidase and 5 vitellogenin-like proteins were common to both adult and pre-adult E/S products. One hundred and seven proteins were identified in the adult E/S but not in the pre-adult E/S and these included serine and cysteine-type endopeptidases, vitellogenins, sphingomyelinase and calreticulin. A total of 27 proteins were identified in pre-adult E/S products but not in adult E/S.

CONCLUSIONS
The assigned functions of these E/S products and the potential roles they play in host-parasite interaction is discussed.

Properties
Additional details for this publication include:
Property NameValue
Journal CountryEngland
Publication TypeJournal Article
Language Abbreng
LanguageEnglish
ISSN1756-3305
Publication ModelElectronic
Elocation10.1186/s13071-018-2885-6
DOI10.1186/s13071-018-2885-6
Journal AbbreviationParasit Vectors
Publication Date2018 May 11
eISSN1756-3305
Cross References
This publication is also available in the following databases:
DatabaseAccession
PMID: PMID:29751843