Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction
International audience Noroviruses, the major cause of acute viral gastroenteritis, are known to bind to histo-blood group antigens (HBGAs), including ABH groups and Lewis-type epitopes, which decorate the surface of erythrocytes and epithelial cells of their host tissues. The biosynthesis of these...
Published in: | Marine Drugs |
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Main Authors: | , , , , , , , , , , , |
Other Authors: | , , , , , , , , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
HAL CCSD
2023
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Subjects: | |
Online Access: | https://hal.univ-lille.fr/hal-04193708 https://hal.univ-lille.fr/hal-04193708/document https://hal.univ-lille.fr/hal-04193708/file/P23.22%20Auger%202023%20Mar%20Drugs.pdf https://doi.org/10.3390/md21060342 |
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ftinserm:oai:HAL:hal-04193708v1 |
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record_format |
openpolar |
institution |
Open Polar |
collection |
Inserm: HAL (Institut national de la santé et de la recherche médicale) |
op_collection_id |
ftinserm |
language |
English |
topic |
Humans Animals Norovirus Crassostrea Ostrea Methylation Ligands Blood Group Antigens Epitopes glycomics norovirus ligands oysters [SDV]Life Sciences [q-bio] [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry |
spellingShingle |
Humans Animals Norovirus Crassostrea Ostrea Methylation Ligands Blood Group Antigens Epitopes glycomics norovirus ligands oysters [SDV]Life Sciences [q-bio] [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry Auger, Audrey Yu, Shin-Yi Guu, Shih-Yun Quéméner, Agnès Euller-Nicolas, Gabriel Ando, Hiromune Desdouits, Marion Le Guyader, Françoise S Khoo, Kay-Hooi Le Pendu, Jacques Chirat, Frederic Guerardel, Yann Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction |
topic_facet |
Humans Animals Norovirus Crassostrea Ostrea Methylation Ligands Blood Group Antigens Epitopes glycomics norovirus ligands oysters [SDV]Life Sciences [q-bio] [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry |
description |
International audience Noroviruses, the major cause of acute viral gastroenteritis, are known to bind to histo-blood group antigens (HBGAs), including ABH groups and Lewis-type epitopes, which decorate the surface of erythrocytes and epithelial cells of their host tissues. The biosynthesis of these antigens is controlled by several glycosyltransferases, the distribution and expression of which varies between tissues and individuals. The use of HBGAs as ligands by viruses is not limited to humans, as many animal species, including oysters, which synthesize similar glycan epitopes that act as a gateway for viruses, become vectors for viral infection in humans. Here, we show that different oyster species synthesize a wide range of -glycans that share histo-blood A-antigens but differ in the expression of other terminal antigens and in their modification by -methyl groups. In particular, we show that the -glycans isolated from and exhibit exquisite methylation patterns in their terminal -acetylgalactosamine and fucose residues in terms of position and number, adding another layer of complexity to the post-translational glycosylation modifications of glycoproteins. Furthermore, modeling of the interactions between norovirus capsid proteins and carbohydrate ligands strongly suggests that methylation has the potential to fine-tune the recognition events of oysters by virus particles. |
author2 |
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF) Université de Lille-Centre National de la Recherche Scientifique (CNRS) Academia Sinica Centre de Recherche en Cancérologie et Immunologie Intégrée Nantes-Angers (CRCI2NA ) Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Nantes Université - UFR de Médecine et des Techniques Médicales (Nantes Univ - UFR MEDECINE) Nantes Université - pôle Santé Nantes Université (Nantes Univ)-Nantes Université (Nantes Univ)-Nantes Université - pôle Santé Nantes Université (Nantes Univ)-Nantes Université (Nantes Univ) Unité Microbiologie Aliment Santé Environnement (MASAE) Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER) Gifu University National Taïwan University (NTU) Immunology and New Concepts in ImmunoTherapy (INCIT) Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Universitaire de Nantes = Nantes University Hospital (CHU Nantes)-Nantes Université - UFR de Médecine et des Techniques Médicales (Nantes Univ - UFR MEDECINE) ANR-19-CE35-0014,GOyAVE,Liaison des virus entériques aux glycines et aux huîtres dans l'environnement littoral(2019) |
format |
Article in Journal/Newspaper |
author |
Auger, Audrey Yu, Shin-Yi Guu, Shih-Yun Quéméner, Agnès Euller-Nicolas, Gabriel Ando, Hiromune Desdouits, Marion Le Guyader, Françoise S Khoo, Kay-Hooi Le Pendu, Jacques Chirat, Frederic Guerardel, Yann |
author_facet |
Auger, Audrey Yu, Shin-Yi Guu, Shih-Yun Quéméner, Agnès Euller-Nicolas, Gabriel Ando, Hiromune Desdouits, Marion Le Guyader, Françoise S Khoo, Kay-Hooi Le Pendu, Jacques Chirat, Frederic Guerardel, Yann |
author_sort |
Auger, Audrey |
title |
Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction |
title_short |
Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction |
title_full |
Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction |
title_fullStr |
Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction |
title_full_unstemmed |
Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction |
title_sort |
species-specific n-glycomes and methylation patterns of oysters crassostrea gigas and ostrea edulis and their possible consequences for the norovirus–hbga interaction |
publisher |
HAL CCSD |
publishDate |
2023 |
url |
https://hal.univ-lille.fr/hal-04193708 https://hal.univ-lille.fr/hal-04193708/document https://hal.univ-lille.fr/hal-04193708/file/P23.22%20Auger%202023%20Mar%20Drugs.pdf https://doi.org/10.3390/md21060342 |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_source |
ISSN: 1660-3397 Marine drugs https://hal.univ-lille.fr/hal-04193708 Marine drugs, 2023, Marine drugs, 21 (6), pp.342. ⟨10.3390/md21060342⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.3390/md21060342 info:eu-repo/semantics/altIdentifier/pmid/37367667 hal-04193708 https://hal.univ-lille.fr/hal-04193708 https://hal.univ-lille.fr/hal-04193708/document https://hal.univ-lille.fr/hal-04193708/file/P23.22%20Auger%202023%20Mar%20Drugs.pdf doi:10.3390/md21060342 PUBMED: 37367667 |
op_rights |
http://creativecommons.org/licenses/by/ info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.3390/md21060342 |
container_title |
Marine Drugs |
container_volume |
21 |
container_issue |
6 |
container_start_page |
342 |
_version_ |
1802643561170075648 |
spelling |
ftinserm:oai:HAL:hal-04193708v1 2024-06-23T07:52:18+00:00 Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction Auger, Audrey Yu, Shin-Yi Guu, Shih-Yun Quéméner, Agnès Euller-Nicolas, Gabriel Ando, Hiromune Desdouits, Marion Le Guyader, Françoise S Khoo, Kay-Hooi Le Pendu, Jacques Chirat, Frederic Guerardel, Yann Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF) Université de Lille-Centre National de la Recherche Scientifique (CNRS) Academia Sinica Centre de Recherche en Cancérologie et Immunologie Intégrée Nantes-Angers (CRCI2NA ) Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Nantes Université - UFR de Médecine et des Techniques Médicales (Nantes Univ - UFR MEDECINE) Nantes Université - pôle Santé Nantes Université (Nantes Univ)-Nantes Université (Nantes Univ)-Nantes Université - pôle Santé Nantes Université (Nantes Univ)-Nantes Université (Nantes Univ) Unité Microbiologie Aliment Santé Environnement (MASAE) Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER) Gifu University National Taïwan University (NTU) Immunology and New Concepts in ImmunoTherapy (INCIT) Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Universitaire de Nantes = Nantes University Hospital (CHU Nantes)-Nantes Université - UFR de Médecine et des Techniques Médicales (Nantes Univ - UFR MEDECINE) ANR-19-CE35-0014,GOyAVE,Liaison des virus entériques aux glycines et aux huîtres dans l'environnement littoral(2019) 2023-06-02 https://hal.univ-lille.fr/hal-04193708 https://hal.univ-lille.fr/hal-04193708/document https://hal.univ-lille.fr/hal-04193708/file/P23.22%20Auger%202023%20Mar%20Drugs.pdf https://doi.org/10.3390/md21060342 en eng HAL CCSD MDPI info:eu-repo/semantics/altIdentifier/doi/10.3390/md21060342 info:eu-repo/semantics/altIdentifier/pmid/37367667 hal-04193708 https://hal.univ-lille.fr/hal-04193708 https://hal.univ-lille.fr/hal-04193708/document https://hal.univ-lille.fr/hal-04193708/file/P23.22%20Auger%202023%20Mar%20Drugs.pdf doi:10.3390/md21060342 PUBMED: 37367667 http://creativecommons.org/licenses/by/ info:eu-repo/semantics/OpenAccess ISSN: 1660-3397 Marine drugs https://hal.univ-lille.fr/hal-04193708 Marine drugs, 2023, Marine drugs, 21 (6), pp.342. ⟨10.3390/md21060342⟩ Humans Animals Norovirus Crassostrea Ostrea Methylation Ligands Blood Group Antigens Epitopes glycomics norovirus ligands oysters [SDV]Life Sciences [q-bio] [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry info:eu-repo/semantics/article Journal articles 2023 ftinserm https://doi.org/10.3390/md21060342 2024-06-10T23:54:29Z International audience Noroviruses, the major cause of acute viral gastroenteritis, are known to bind to histo-blood group antigens (HBGAs), including ABH groups and Lewis-type epitopes, which decorate the surface of erythrocytes and epithelial cells of their host tissues. The biosynthesis of these antigens is controlled by several glycosyltransferases, the distribution and expression of which varies between tissues and individuals. The use of HBGAs as ligands by viruses is not limited to humans, as many animal species, including oysters, which synthesize similar glycan epitopes that act as a gateway for viruses, become vectors for viral infection in humans. Here, we show that different oyster species synthesize a wide range of -glycans that share histo-blood A-antigens but differ in the expression of other terminal antigens and in their modification by -methyl groups. In particular, we show that the -glycans isolated from and exhibit exquisite methylation patterns in their terminal -acetylgalactosamine and fucose residues in terms of position and number, adding another layer of complexity to the post-translational glycosylation modifications of glycoproteins. Furthermore, modeling of the interactions between norovirus capsid proteins and carbohydrate ligands strongly suggests that methylation has the potential to fine-tune the recognition events of oysters by virus particles. Article in Journal/Newspaper Crassostrea gigas Inserm: HAL (Institut national de la santé et de la recherche médicale) Marine Drugs 21 6 342 |