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

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 produ...

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Published inParasites & vectors Vol. 11; no. 1; p. 294
Main Authors Hamilton, Scott, McLean, Kevin, Monaghan, Sean J, McNair, Carol, Inglis, Neil F, McDonald, Hazel, Adams, Sandra, Richards, Randolph, Roy, William, Smith, Patrick, Bron, James, Nisbet, Alasdair J, Knox, David
Format Journal Article
LanguageEnglish
Published England BioMed Central Ltd 11.05.2018
BioMed Central
BMC
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Summary: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. 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. 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. The assigned functions of these E/S products and the potential roles they play in host-parasite interaction is discussed.
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ISSN:1756-3305
1756-3305
DOI:10.1186/s13071-018-2885-6