Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction
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...
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ftmdpi:oai:mdpi.com:/1660-3397/21/6/342/ 2023-08-20T04:06:02+02:00 Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction Audrey Auger Shin-Yi Yu Shih-Yun Guu Agnès Quéméner Gabriel Euller-Nicolas Hiromune Ando Marion Desdouits Françoise S. Le Guyader Kay-Hooi Khoo Jacques Le Pendu Frederic Chirat Yann Guerardel agris 2023-06-02 application/pdf https://doi.org/10.3390/md21060342 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/md21060342 https://creativecommons.org/licenses/by/4.0/ Marine Drugs; Volume 21; Issue 6; Pages: 342 glycomics norovirus ligands oysters methylation Text 2023 ftmdpi https://doi.org/10.3390/md21060342 2023-08-01T10:20:08Z 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 N-glycans that share histo-blood A-antigens but differ in the expression of other terminal antigens and in their modification by O-methyl groups. In particular, we show that the N-glycans isolated from Crassostrea gigas and Ostrea edulis exhibit exquisite methylation patterns in their terminal N-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. Text Crassostrea gigas MDPI Open Access Publishing Marine Drugs 21 6 342 |
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MDPI Open Access Publishing |
op_collection_id |
ftmdpi |
language |
English |
topic |
glycomics norovirus ligands oysters methylation |
spellingShingle |
glycomics norovirus ligands oysters methylation Audrey Auger Shin-Yi Yu Shih-Yun Guu Agnès Quéméner Gabriel Euller-Nicolas Hiromune Ando Marion Desdouits Françoise S. Le Guyader Kay-Hooi Khoo Jacques Le Pendu Frederic Chirat Yann Guerardel 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 |
glycomics norovirus ligands oysters methylation |
description |
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 N-glycans that share histo-blood A-antigens but differ in the expression of other terminal antigens and in their modification by O-methyl groups. In particular, we show that the N-glycans isolated from Crassostrea gigas and Ostrea edulis exhibit exquisite methylation patterns in their terminal N-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. |
format |
Text |
author |
Audrey Auger Shin-Yi Yu Shih-Yun Guu Agnès Quéméner Gabriel Euller-Nicolas Hiromune Ando Marion Desdouits Françoise S. Le Guyader Kay-Hooi Khoo Jacques Le Pendu Frederic Chirat Yann Guerardel |
author_facet |
Audrey Auger Shin-Yi Yu Shih-Yun Guu Agnès Quéméner Gabriel Euller-Nicolas Hiromune Ando Marion Desdouits Françoise S. Le Guyader Kay-Hooi Khoo Jacques Le Pendu Frederic Chirat Yann Guerardel |
author_sort |
Audrey Auger |
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 |
Multidisciplinary Digital Publishing Institute |
publishDate |
2023 |
url |
https://doi.org/10.3390/md21060342 |
op_coverage |
agris |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_source |
Marine Drugs; Volume 21; Issue 6; Pages: 342 |
op_relation |
https://dx.doi.org/10.3390/md21060342 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/md21060342 |
container_title |
Marine Drugs |
container_volume |
21 |
container_issue |
6 |
container_start_page |
342 |
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1774716952013438976 |