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Sci Rep. 2018 Aug 28;8(1):12961. doi: 10.1038/s41598-018-31005-4.

Histo-blood group antigen-binding specificities of human rotaviruses are associated with gastroenteritis but not with in vitro infection.

Author information

CRCINA, Inserm, Université d'Angers, Université de Nantes, Nantes, France.
Plateforme P2R « Production de protéines recombinantes », SFR Sante F. Bonamy-IRS-UN, Université de Nantes, INSERM, CNRS, CHU Nantes, Nantes, France.
Biofortis, Mérieux NutriSciences, Nantes, France.
Institute of Bioorganic Chemistry RAS, Moscow, Russia.
Division of Molecular Virology, Medical Faculty, University of Linköping, Linköping, Sweden.
Division of Infectious Diseases, Department of Medicine Solna, Karolinska Institute, Stockholm, Sweden.
Oniris, Ecole Nationale Vétérinaire, Agroalimentaire et de l'Alimentation, Nantes, France.
CRCINA, Inserm, Université d'Angers, Université de Nantes, Nantes, France.


Human strains of rotavirus A (RVAs) recognize fucosylated glycans belonging to histo-blood group antigens (HBGAs) through their spike protein VP8*. Lack of these ligands due to genetic polymorphisms is associated with resistance to gastroenteritis caused by P[8] genotype RVAs. With the aim to delineate the contribution of HBGAs in the process, we analyzed the glycan specificity of VP8* proteins from various P genotypes. Binding to saliva of VP8* from P[8] and P[4] genotypes required expression of both FUT2 and FUT3 enzymes, whilst binding of VP8* from the P[14] genotype required FUT2 and A enzymes. We further defined a glycan motif, GlcNAcβ3Galβ4GlcNAc, recognized by P[6] clinical strains. Conversion into Lewis antigens by the FUT3 enzyme impaired recognition, explaining their lower binding to saliva of Lewis positive phenotype. In addition, the presence of neutralizing antibodies was associated with the presence of the FUT2 wild type allele in sera from young healthy adults. Nonetheless, in vitro infection of transformed cell lines was independent of HBGAs expression, indicating that HBGAs are not human RV receptors. The match between results from saliva-based binding assays and the epidemiological data indicates that the polymorphism of human HBGAs controls susceptibility to RVAs, although the exact mechanism remains unclear.

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