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Appears in Collections:Aquaculture Journal Articles
Peer Review Status: Refereed
Title: Characterisation of proteins in excretory/secretory products collected from salmon lice, Lepeophtheirus salmonis
Author(s): Hamilton, Scott
McLean, Kevin
Monaghan, Sean
McNair, Carol
Inglis, Neil F
McDonald, Hazel C
Adams, Alexandra
Richards, Randolph
Roy, William
Smith, Patrick
Bron, James
Nisbet, Alasdair
Knox, David
Keywords: Lepeophtheirus salmonis
Excretory/secretory (E/S) products
Sea lice
Issue Date: 11-May-2018
Citation: Hamilton S, McLean K, Monaghan S, McNair C, Inglis NF, McDonald HC, Adams A, Richards R, Roy W, Smith P, Bron J, Nisbet A & Knox D (2018) Characterisation of proteins in excretory/secretory products collected from salmon lice, Lepeophtheirus salmonis, Parasites and Vectors, 11 (1), Art. No.: 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.
DOI Link: 10.1186/s13071-018-2885-6
Rights: © The Author(s). 2018 This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (, which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( applies to the data made available in this article, unless otherwise stated.

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