FN Archimer Export Format
PT J
TI Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction
BT 
AF Auger, Audrey
   Yu, Shin-Yi
   Guu, Shih-Yun
   Quéméner, Agnès
   EULLER, Gabriel
   Ando, Hiromune
   DESDOUITS, Marion
   LE GUYADER, Soizick
   Khoo, Kay-Hooi
   Le Pendu, Jacques
   Chirat, Frédéric
   Guerardel, Yann
AS 1:1;2:1;3:2;4:3;5:4;6:5;7:4;8:4;9:2,6;10:7;11:1;12:1,5;
FF 1:;2:;3:;4:;5:PDG-RBE-MASAE-LSEM;6:;7:PDG-RBE-MASAE-LSEM;8:PDG-RBE-MASAE-LSEM;9:;10:;11:;12:;
C1 Univ. Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France
   Institute of Biological Chemistry, Academia Sinica, Nangang, Taipei 11529, Taiwan
   CRCI2NA, Inserm UMR 1307, CNRS UMR 6075, Nantes Université, Université d’Angers, F-44000 Nantes, France
   MASAE Microbiologie Aliment Santé Environnement, Ifremer, BP 21105, 44311 Nantes, France
   Institute for Glyco-core Research (iGCORE), Gifu University, Gifu 501-1193, Japan
   Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan
   Immunology and New Concepts in ImmunoTherapy, Nantes Université, Inserm, CNRS, UMR 1302/EMR6001, 44200 Nantes, France
C2 UNIV LILLE, FRANCE
   ACAD SINICA, TAIWAN
   INSERM, FRANCE
   IFREMER, FRANCE
   UNIV GIFU, JAPAN
   UNIV NATL TAIWAN, TAIWAN
   UNIV NANTES, FRANCE
SI NANTES
SE PDG-RBE-MASAE-LSEM
IN WOS Ifremer UPR
   DOAJ
   copubli-france
   copubli-univ-france
   copubli-int-hors-europe
IF 5.4
TC 0
UR https://archimer.ifremer.fr/doc/00840/95215/102930.pdf
   https://archimer.ifremer.fr/doc/00840/95215/102931.zip
LA English
DT Article
DE ;glycomics;norovirus ligands;oysters;methylation
AB 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. 
PY 2023
PD JUL
SO Marine Drugs
SN 1660-3397
PU MDPI
VL 21
IS 6
UT 001017450400001
ID 95215
ER

EF