Carol McNair
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Carol McNair has a total of 12 co-authors. Here are the top co-authors by number of shared publications:
- Alasdair J. Nisbet
Department of Vaccines and Diagnostics, Moredun Research Institute, Edinburgh, UK
1 shared publication - David Knox
Moredun Research Institute, Pentlands Sciences Park, Bush Loan, EH26 0PZ, Penicuik, Scotland, UK
1 shared publication - Hazel McDonald
Institute of Aquaculture, School of Natural Sciences, University of Stirling, FK9 4LA, Stirling, Scotland, UK
1 shared publication - James Emmanuel Bron
Institute of Aquaculture, University of Stirling, Stirling, Scotland, UK
1 shared publication - Kevin McLean
Moredun Proteomics Facility, Moredun Research Institute, Pentland Science Park, Bush Loan, Penicuik, Midlothian, EH26 0PZ, UK
1 shared publication - Neil F. Inglis
Moredun Proteomics Facility, Moredun Research Institute, Pentland Science Park, Bush Loan, Penicuik, Midlothian, EH26 0PZ, UK
1 shared publication
Latest Publications
- Open Access
- 11 May 2018
- Published by Springer Nature in Parasites & Vectors
- Vol. 11 (1) , 294
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 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.
- 11 May 2018
- Published by Springer Nature in Parasites & Vectors
- Vol. 11 (1) , 294
Open AccessCharacterisation 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 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.