Titre :

Species-Specific -Glycomes and Methylation Patterns of Oysters and and Their Possible Consequences for the Norovirus-HBGA Interaction.

Auteur(s) :

Auger, Audrey [Auteur]
Yu, Shin-Yi [Auteur]
Lille Neurosciences & Cognition (LilNCog) - U 1172
Guu, Shih-Yun [Auteur]
Quéméner, Agnès [Auteur]
Euller-Nicolas, Gabriel [Auteur]
Ando, Hiromune [Auteur]
Desdouits, Marion [Auteur]
Le Guyader, Françoise S [Auteur]
Khoo, Kay-Hooi [Auteur]
Le Pendu, Jacques [Auteur]
Chirat, Frederic [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Titre de la revue :

Marine Drugs

Nom court de la revue :

Mar Drugs

Numéro :

21

Date de publication :

2023-06-02

ISSN :

1660-3397

Mot(s)-clé(s) en anglais :

Humans
Animals
Norovirus
Crassostrea
Ostrea
Methylation
Ligands
Blood Group Antigens
Epitopes
glycomics
methylation
norovirus ligands
oysters

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

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 ...
Lire la suite >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.Lire moins >

Langue :

Anglais

Audience :

Non spécifiée

Établissement(s) :

Université de Lille
CNRS

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

Chemical Glycobiology

Date de dépôt :

2023-07-19T08:56:54Z