Salmon louse labial gland enzymes: implications for host settlement and immune modulation

Salmon louse (Lepeophtheirus salmonis) is a skin- and blood-feeding ectoparasite, infesting salmonids. While feeding, labial gland proteins from the salmon louse may be deposited on the Atlantic salmon (Salmo salar) skin. Previously characterized labial gland proteins are involved in anti-coagulatio...

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Published in:Frontiers in Genetics
Main Authors: Midtbø, Helena Marie Doherty, Eichner, Christiane, Hamre, Lars Are, Dondrup, Michael, Flesland, Linn, Tysseland, Kristoffer Helland, Kongshaug, Heidi, Borchel, Andreas, Nilsen, Frank, Øvergård, Aina-Cathrine
Format: Article in Journal/Newspaper
Language:English
Published: Frontiers 2024
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Online Access:https://hdl.handle.net/11250/3127446
https://doi.org/10.3389/fgene.2023.1303898
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spelling ftunivbergen:oai:bora.uib.no:11250/3127446 2024-05-19T07:37:45+00:00 Salmon louse labial gland enzymes: implications for host settlement and immune modulation Midtbø, Helena Marie Doherty Eichner, Christiane Hamre, Lars Are Dondrup, Michael Flesland, Linn Tysseland, Kristoffer Helland Kongshaug, Heidi Borchel, Andreas Nilsen, Frank Øvergård, Aina-Cathrine 2024 application/pdf https://hdl.handle.net/11250/3127446 https://doi.org/10.3389/fgene.2023.1303898 eng eng Frontiers urn:issn:1664-8021 https://hdl.handle.net/11250/3127446 https://doi.org/10.3389/fgene.2023.1303898 cristin:2229519 Frontiers in Genetics. 2024, 14, 1303898. Navngivelse 4.0 Internasjonal http://creativecommons.org/licenses/by/4.0/deed.no Copyright 2024 The Author(s) 1303898 Frontiers in Genetics 14 Journal article Peer reviewed 2024 ftunivbergen https://doi.org/10.3389/fgene.2023.1303898 2024-04-23T23:32:31Z Salmon louse (Lepeophtheirus salmonis) is a skin- and blood-feeding ectoparasite, infesting salmonids. While feeding, labial gland proteins from the salmon louse may be deposited on the Atlantic salmon (Salmo salar) skin. Previously characterized labial gland proteins are involved in anti-coagulation and may contribute to inhibiting Atlantic salmon from mounting a sufficient immune response against the ectoparasite. As labial gland proteins seem to be important in the host–parasite interaction, we have, therefore, identified and characterized ten enzymes localized to the labial gland. They are a large group of astacins named L. salmonis labial gland astacin 1–8 (LsLGA 1–8), one serine protease named L. salmonis labial gland serine protease 1 (LsLGSP1), and one apyrase named L. salmonis labial gland apyrase 1 (LsLGAp1). Protein domain predictions showed that LsLGA proteins all have N-terminal ShK domains, which may bind to potassium channels targeting the astacins to its substrate. LsLGA1 and -4 are, in addition, expressed in another gland type, whose secrete also meets the host–parasite interface. This suggests that LsLGA proteins may have an anti-microbial function and may prevent secondary infections in the wounds. LsLGAp1 is predicted to hydrolyze ATP or AMP and is, thereby, suggested to have an immune dampening function. In a knockdown study targeting LsLGSP1, a significant increase in IL-8 and MMP13 at the skin infestation site was seen under LsLGSP1 knockdown salmon louse compared to the control, suggesting that LsLGSP1 may have an anti-inflammatory effect. Moreover, most of the identified labial gland proteins are expressed in mature copepodids prior to host settlement, are not regulated by starvation, and are expressed at similar or higher levels in lice infesting the salmon louse-resistant pink salmon (Oncorhynchus gorbuscha). This study, thereby, emphasizes the importance of labial gland proteins for host settlement and their immune dampening function. This work can further contribute to anti-salmon ... Article in Journal/Newspaper Atlantic salmon Oncorhynchus gorbuscha Pink salmon Salmo salar University of Bergen: Bergen Open Research Archive (BORA-UiB) Frontiers in Genetics 14
institution Open Polar
collection University of Bergen: Bergen Open Research Archive (BORA-UiB)
op_collection_id ftunivbergen
language English
description Salmon louse (Lepeophtheirus salmonis) is a skin- and blood-feeding ectoparasite, infesting salmonids. While feeding, labial gland proteins from the salmon louse may be deposited on the Atlantic salmon (Salmo salar) skin. Previously characterized labial gland proteins are involved in anti-coagulation and may contribute to inhibiting Atlantic salmon from mounting a sufficient immune response against the ectoparasite. As labial gland proteins seem to be important in the host–parasite interaction, we have, therefore, identified and characterized ten enzymes localized to the labial gland. They are a large group of astacins named L. salmonis labial gland astacin 1–8 (LsLGA 1–8), one serine protease named L. salmonis labial gland serine protease 1 (LsLGSP1), and one apyrase named L. salmonis labial gland apyrase 1 (LsLGAp1). Protein domain predictions showed that LsLGA proteins all have N-terminal ShK domains, which may bind to potassium channels targeting the astacins to its substrate. LsLGA1 and -4 are, in addition, expressed in another gland type, whose secrete also meets the host–parasite interface. This suggests that LsLGA proteins may have an anti-microbial function and may prevent secondary infections in the wounds. LsLGAp1 is predicted to hydrolyze ATP or AMP and is, thereby, suggested to have an immune dampening function. In a knockdown study targeting LsLGSP1, a significant increase in IL-8 and MMP13 at the skin infestation site was seen under LsLGSP1 knockdown salmon louse compared to the control, suggesting that LsLGSP1 may have an anti-inflammatory effect. Moreover, most of the identified labial gland proteins are expressed in mature copepodids prior to host settlement, are not regulated by starvation, and are expressed at similar or higher levels in lice infesting the salmon louse-resistant pink salmon (Oncorhynchus gorbuscha). This study, thereby, emphasizes the importance of labial gland proteins for host settlement and their immune dampening function. This work can further contribute to anti-salmon ...
format Article in Journal/Newspaper
author Midtbø, Helena Marie Doherty
Eichner, Christiane
Hamre, Lars Are
Dondrup, Michael
Flesland, Linn
Tysseland, Kristoffer Helland
Kongshaug, Heidi
Borchel, Andreas
Nilsen, Frank
Øvergård, Aina-Cathrine
spellingShingle Midtbø, Helena Marie Doherty
Eichner, Christiane
Hamre, Lars Are
Dondrup, Michael
Flesland, Linn
Tysseland, Kristoffer Helland
Kongshaug, Heidi
Borchel, Andreas
Nilsen, Frank
Øvergård, Aina-Cathrine
Salmon louse labial gland enzymes: implications for host settlement and immune modulation
author_facet Midtbø, Helena Marie Doherty
Eichner, Christiane
Hamre, Lars Are
Dondrup, Michael
Flesland, Linn
Tysseland, Kristoffer Helland
Kongshaug, Heidi
Borchel, Andreas
Nilsen, Frank
Øvergård, Aina-Cathrine
author_sort Midtbø, Helena Marie Doherty
title Salmon louse labial gland enzymes: implications for host settlement and immune modulation
title_short Salmon louse labial gland enzymes: implications for host settlement and immune modulation
title_full Salmon louse labial gland enzymes: implications for host settlement and immune modulation
title_fullStr Salmon louse labial gland enzymes: implications for host settlement and immune modulation
title_full_unstemmed Salmon louse labial gland enzymes: implications for host settlement and immune modulation
title_sort salmon louse labial gland enzymes: implications for host settlement and immune modulation
publisher Frontiers
publishDate 2024
url https://hdl.handle.net/11250/3127446
https://doi.org/10.3389/fgene.2023.1303898
genre Atlantic salmon
Oncorhynchus gorbuscha
Pink salmon
Salmo salar
genre_facet Atlantic salmon
Oncorhynchus gorbuscha
Pink salmon
Salmo salar
op_source 1303898
Frontiers in Genetics
14
op_relation urn:issn:1664-8021
https://hdl.handle.net/11250/3127446
https://doi.org/10.3389/fgene.2023.1303898
cristin:2229519
Frontiers in Genetics. 2024, 14, 1303898.
op_rights Navngivelse 4.0 Internasjonal
http://creativecommons.org/licenses/by/4.0/deed.no
Copyright 2024 The Author(s)
op_doi https://doi.org/10.3389/fgene.2023.1303898
container_title Frontiers in Genetics
container_volume 14
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