Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction

• Main Authors: 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
• Other Authors: Université de Lille, CNRS, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 UGSF, Academia Sinica, Centre de Recherche en Cancérologie et Immunologie Intégrée Nantes-Angers CRCI2NA, Microbiologie Aliment Santé Environnement MASAE, Gifu University, National Taïwan University NTU, Immunology and New Concepts in ImmunoTherapy INCIT, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
• Format: Article in Journal/Newspaper
• Language: English
• Published: MDPI 2023
• Subjects: Humans;Animals;Norovirus;Crassostrea;Ostrea;Methylation;Ligands;Blood Group Antigens;Epitopes;glycomics;methylation;norovirus ligands;oysters; Crassostrea gigas
• Online Access: https://hdl.handle.net/20.500.12210/86228

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. 21;6