Species-Specific <i>N</i>-Glycomes and Methylation Patterns of Oysters <i>Crassostrea gigas</i> and <i>Ostrea edulis</i> 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
Affiliations
Audrey Auger
Univ. Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France
Shin-Yi Yu
Univ. Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France
Shih-Yun Guu
Institute of Biological Chemistry, Academia Sinica, Nangang, Taipei 11529, Taiwan
Agnès Quéméner
Nantes Université, Inserm UMR 1307, CNRS UMR 6075, Université d’Angers, CRCI2NA, F-44000 Nantes, France
Gabriel Euller-Nicolas
MASAE Microbiologie Aliment Santé Environnement, Ifremer, BP 21105, 44311 Nantes, France
Hiromune Ando
Institute for Glyco-core Research (iGCORE), Gifu University, Gifu 501-1193, Japan
Marion Desdouits
MASAE Microbiologie Aliment Santé Environnement, Ifremer, BP 21105, 44311 Nantes, France
Françoise S. Le Guyader
MASAE Microbiologie Aliment Santé Environnement, Ifremer, BP 21105, 44311 Nantes, France
Kay-Hooi Khoo
Institute of Biological Chemistry, Academia Sinica, Nangang, Taipei 11529, Taiwan
Jacques Le Pendu
Immunology and New Concepts in ImmunoTherapy, Nantes Université, Inserm, CNRS, UMR 1302/EMR6001, 44200 Nantes, France
Frederic Chirat
Univ. Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France
Yann Guerardel
Univ. Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France
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.