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Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon

Amoebic gill disease (AGD) causes poor performance and death in salmonids. Mucins are mainly comprised by carbohydrates and are main components of the mucus covering the gill. Since glycans regulate pathogen binding and growth, glycosylation changes may affect susceptibility to primary and secondary...

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Autores principales: Benktander, John, Padra, János T., Maynard, Ben, Birchenough, George, Botwright, Natasha A., McCulloch, Russel, Wynne, James W., Sharba, Sinan, Sundell, Kristina, Sundh, Henrik, Lindén, Sara K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7768351/
https://www.ncbi.nlm.nih.gov/pubmed/33256221
http://dx.doi.org/10.3390/microorganisms8121871
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author Benktander, John
Padra, János T.
Maynard, Ben
Birchenough, George
Botwright, Natasha A.
McCulloch, Russel
Wynne, James W.
Sharba, Sinan
Sundell, Kristina
Sundh, Henrik
Lindén, Sara K.
author_facet Benktander, John
Padra, János T.
Maynard, Ben
Birchenough, George
Botwright, Natasha A.
McCulloch, Russel
Wynne, James W.
Sharba, Sinan
Sundell, Kristina
Sundh, Henrik
Lindén, Sara K.
author_sort Benktander, John
collection PubMed
description Amoebic gill disease (AGD) causes poor performance and death in salmonids. Mucins are mainly comprised by carbohydrates and are main components of the mucus covering the gill. Since glycans regulate pathogen binding and growth, glycosylation changes may affect susceptibility to primary and secondary infections. We investigated gill mucin O-glycosylation from Atlantic salmon with and without AGD using liquid chromatography–mass spectrometry. Gill mucin glycans were larger and more complex, diverse and fucosylated than skin mucins. Confocal microscopy revealed that fucosylated mucus coated sialylated mucus strands in ex vivo gill mucus. Terminal HexNAcs were more abundant among O-glycans from AGD-affected Atlantic salmon, whereas core 1 structures and structures with acidic moieties such as N-acetylneuraminic acid (NeuAc) and sulfate groups were less abundant compared to non-infected fish. The fucosylated and NeuAc-containing O-glycans were inversely proportional, with infected fish on the lower scale of NeuAc abundance and high on fucosylated structures. The fucosylated epitopes were of three types: Fuc-HexNAc-R, Gal-[Fuc-]HexNAc-R and HexNAc-[Fuc-]HexNAc-R. These blood group-like structures could be an avenue to diversify the glycan repertoire to limit infection in the exposed gills. Furthermore, care must be taken when using skin mucus as proxy for gill mucus, as gill mucins are distinctly different from skin mucins.
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spelling pubmed-77683512020-12-29 Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon Benktander, John Padra, János T. Maynard, Ben Birchenough, George Botwright, Natasha A. McCulloch, Russel Wynne, James W. Sharba, Sinan Sundell, Kristina Sundh, Henrik Lindén, Sara K. Microorganisms Article Amoebic gill disease (AGD) causes poor performance and death in salmonids. Mucins are mainly comprised by carbohydrates and are main components of the mucus covering the gill. Since glycans regulate pathogen binding and growth, glycosylation changes may affect susceptibility to primary and secondary infections. We investigated gill mucin O-glycosylation from Atlantic salmon with and without AGD using liquid chromatography–mass spectrometry. Gill mucin glycans were larger and more complex, diverse and fucosylated than skin mucins. Confocal microscopy revealed that fucosylated mucus coated sialylated mucus strands in ex vivo gill mucus. Terminal HexNAcs were more abundant among O-glycans from AGD-affected Atlantic salmon, whereas core 1 structures and structures with acidic moieties such as N-acetylneuraminic acid (NeuAc) and sulfate groups were less abundant compared to non-infected fish. The fucosylated and NeuAc-containing O-glycans were inversely proportional, with infected fish on the lower scale of NeuAc abundance and high on fucosylated structures. The fucosylated epitopes were of three types: Fuc-HexNAc-R, Gal-[Fuc-]HexNAc-R and HexNAc-[Fuc-]HexNAc-R. These blood group-like structures could be an avenue to diversify the glycan repertoire to limit infection in the exposed gills. Furthermore, care must be taken when using skin mucus as proxy for gill mucus, as gill mucins are distinctly different from skin mucins. MDPI 2020-11-26 /pmc/articles/PMC7768351/ /pubmed/33256221 http://dx.doi.org/10.3390/microorganisms8121871 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Benktander, John
Padra, János T.
Maynard, Ben
Birchenough, George
Botwright, Natasha A.
McCulloch, Russel
Wynne, James W.
Sharba, Sinan
Sundell, Kristina
Sundh, Henrik
Lindén, Sara K.
Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon
title Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon
title_full Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon
title_fullStr Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon
title_full_unstemmed Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon
title_short Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon
title_sort gill mucus and gill mucin o-glycosylation in healthy and amebic gill disease-affected atlantic salmon
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7768351/
https://www.ncbi.nlm.nih.gov/pubmed/33256221
http://dx.doi.org/10.3390/microorganisms8121871
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