Aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine
ABSTRACTCarbohydrates can both protect against infection and act as targets promoting infection. Mucins are major components of the slimy mucus layer covering the fish epithelia. Mucins can act as decoys for intimate pathogen interaction with the host afforded by binding to glycosphingolipids in the...
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Taylor & Francis Group
2022
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Online Access: | https://doi.org/10.1080/21505594.2022.2132056 https://doaj.org/article/d0b4b50cfb394824a9d6e89f776d0e8b |
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ftdoajarticles:oai:doaj.org/article:d0b4b50cfb394824a9d6e89f776d0e8b 2023-05-15T15:30:32+02:00 Aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine John Benktander Henrik Sundh Sinan Sharba Susann Teneberg Sara K. Lindén 2022-12-01T00:00:00Z https://doi.org/10.1080/21505594.2022.2132056 https://doaj.org/article/d0b4b50cfb394824a9d6e89f776d0e8b EN eng Taylor & Francis Group https://www.tandfonline.com/doi/10.1080/21505594.2022.2132056 https://doaj.org/toc/2150-5594 https://doaj.org/toc/2150-5608 doi:10.1080/21505594.2022.2132056 2150-5608 2150-5594 https://doaj.org/article/d0b4b50cfb394824a9d6e89f776d0e8b Virulence, Vol 13, Iss 1, Pp 1741-1751 (2022) Glycosphingolipid Atlantic salmon host–pathogen interaction Aeromonas salmonicida mucin glycan Infectious and parasitic diseases RC109-216 article 2022 ftdoajarticles https://doi.org/10.1080/21505594.2022.2132056 2022-12-30T20:06:26Z ABSTRACTCarbohydrates can both protect against infection and act as targets promoting infection. Mucins are major components of the slimy mucus layer covering the fish epithelia. Mucins can act as decoys for intimate pathogen interaction with the host afforded by binding to glycosphingolipids in the host cell membrane. We isolated and characterized glycosphingolipids from Atlantic salmon skin, gill, stomach, pyloric caeca, and intestine. We characterized the glycosphingolipids using liquid chromatography – mass spectrometry and tandem mass spectrometry and the glycan repertoire was compared with the glycan repertoire of mucins from the same epithelia. We also investigated Aeromonas salmonicida binding using chromatogram and microtiter well based binding assays. We identified 29 glycosphingolipids. All detected acid glycans were of the ganglio-series (unless shorter) and showed a high degree of polysialylation. The non-acid glycans were mostly composed of the neolacto, globo, and ganglio core structures. The glycosphingolipid repertoire differed between epithelia and the proportion of the terminal moieties of the glycosphingolipids did not reflect the terminal moieties on the mucins from the same epithelia. A. salmonicida did not bind the Atlantic salmon glycosphingolipids. Instead, we identified that A. salmonicida binding to sialic acid occurred to α2–6 Neu5Ac but not to α2–3 Neu5Ac. α2–6 Neu5Ac was present on mucins whereas mainly α2–3 Neu5Ac was found on the glycosphingolipids, explaining the difference in A. salmonicida binding ability between these host glycoconjugates. A. salmonicida´s ability to bind to Atlantic salmon mucins, but not the glycosphingolipids, is likely part of the host defence against this pathogen. Article in Journal/Newspaper Atlantic salmon Directory of Open Access Journals: DOAJ Articles Virulence 13 1 1741 1751 |
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Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Glycosphingolipid Atlantic salmon host–pathogen interaction Aeromonas salmonicida mucin glycan Infectious and parasitic diseases RC109-216 |
spellingShingle |
Glycosphingolipid Atlantic salmon host–pathogen interaction Aeromonas salmonicida mucin glycan Infectious and parasitic diseases RC109-216 John Benktander Henrik Sundh Sinan Sharba Susann Teneberg Sara K. Lindén Aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine |
topic_facet |
Glycosphingolipid Atlantic salmon host–pathogen interaction Aeromonas salmonicida mucin glycan Infectious and parasitic diseases RC109-216 |
description |
ABSTRACTCarbohydrates can both protect against infection and act as targets promoting infection. Mucins are major components of the slimy mucus layer covering the fish epithelia. Mucins can act as decoys for intimate pathogen interaction with the host afforded by binding to glycosphingolipids in the host cell membrane. We isolated and characterized glycosphingolipids from Atlantic salmon skin, gill, stomach, pyloric caeca, and intestine. We characterized the glycosphingolipids using liquid chromatography – mass spectrometry and tandem mass spectrometry and the glycan repertoire was compared with the glycan repertoire of mucins from the same epithelia. We also investigated Aeromonas salmonicida binding using chromatogram and microtiter well based binding assays. We identified 29 glycosphingolipids. All detected acid glycans were of the ganglio-series (unless shorter) and showed a high degree of polysialylation. The non-acid glycans were mostly composed of the neolacto, globo, and ganglio core structures. The glycosphingolipid repertoire differed between epithelia and the proportion of the terminal moieties of the glycosphingolipids did not reflect the terminal moieties on the mucins from the same epithelia. A. salmonicida did not bind the Atlantic salmon glycosphingolipids. Instead, we identified that A. salmonicida binding to sialic acid occurred to α2–6 Neu5Ac but not to α2–3 Neu5Ac. α2–6 Neu5Ac was present on mucins whereas mainly α2–3 Neu5Ac was found on the glycosphingolipids, explaining the difference in A. salmonicida binding ability between these host glycoconjugates. A. salmonicida´s ability to bind to Atlantic salmon mucins, but not the glycosphingolipids, is likely part of the host defence against this pathogen. |
format |
Article in Journal/Newspaper |
author |
John Benktander Henrik Sundh Sinan Sharba Susann Teneberg Sara K. Lindén |
author_facet |
John Benktander Henrik Sundh Sinan Sharba Susann Teneberg Sara K. Lindén |
author_sort |
John Benktander |
title |
Aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine |
title_short |
Aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine |
title_full |
Aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine |
title_fullStr |
Aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine |
title_full_unstemmed |
Aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine |
title_sort |
aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine |
publisher |
Taylor & Francis Group |
publishDate |
2022 |
url |
https://doi.org/10.1080/21505594.2022.2132056 https://doaj.org/article/d0b4b50cfb394824a9d6e89f776d0e8b |
genre |
Atlantic salmon |
genre_facet |
Atlantic salmon |
op_source |
Virulence, Vol 13, Iss 1, Pp 1741-1751 (2022) |
op_relation |
https://www.tandfonline.com/doi/10.1080/21505594.2022.2132056 https://doaj.org/toc/2150-5594 https://doaj.org/toc/2150-5608 doi:10.1080/21505594.2022.2132056 2150-5608 2150-5594 https://doaj.org/article/d0b4b50cfb394824a9d6e89f776d0e8b |
op_doi |
https://doi.org/10.1080/21505594.2022.2132056 |
container_title |
Virulence |
container_volume |
13 |
container_issue |
1 |
container_start_page |
1741 |
op_container_end_page |
1751 |
_version_ |
1766360980732772352 |