Glycobiology Advance Access originally published online on December 3, 2008
Glycobiology 2009 19(3):309-320; doi:10.1093/glycob/cwn139
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Human noroviruses recognize sialyl Lewis x neoglycoprotein
2 Department of Clinical Chemistry and Transfusion Medicine, Sahlgrenska University Hospital, Göteborg
3 Division of Molecular Virology, University of Linköping, Sweden
4 INSERM, U892, Nantes, France; Université de Nantes
5 National Veterinary School of Nantes, Nantes, France
1 To whom correspondence should be addressed: Tel: +46-31-342-1330; Fax: +46-31-828458; e-mail: goran.larson{at}clinchem.gu.se
Received on October 6, 2008; revised on December 1, 2008; accepted on December 1, 2008
The carbohydrate binding characteristics of a norovirus GII.3 (Chron1) and a GII.4 (Dijon) strain were investigated using virus-like particles (VLPs) and saliva samples from 81 individuals genotyped for FUT2 (secretor) and FUT3 (Lewis) and phenotyped for ABO and Lewis blood groups. The two VLPs showed a typical secretor-gene-dependent binding and bound significantly stronger to saliva from A, B, and AB than from O individuals (P < 0.0001 and P < 0.001) but did not bind to any samples from secretor-negative individuals. The GII.3 strain showed larger interindividual variation and bound stronger to saliva from B than from A2 secretors (P < 0.01). When assaying for binding to neoglycoproteins, the GII.3 and GII.4 strains were compared with the Norwalk GI.1 prototype strain. Although all three strains bound to Lewis b (and H type 1 chain) glycoconjugates, only the two GII strains showed an additional binding to sialyl Lewis x. This novel binding was specific since the VLPs did not bind to structural analogs, e.g., Lewis x or sialyl Lewis a, but only to sialyl Lewis x, sialyl diLewis x and sialylated type 2 chain conjugates. In inhibition experiments, the sialyl Lewis x conjugate was the most potent inhibitor. The minimal requirement for this potential receptor structure is Neu5Ac
3Galβ4(Fuc3)GlcNAcβ3Galβ- where Fuc is not absolutely necessary for binding. Our study shows that some human norovirus GII strains have at least two binding specificities: one secretor-gene-dependent related to 1,2-fucosylated carbohydrates and another related to 2,3-sialylated carbohydrates of the type 2 chain, e.g., sialyl Lewis x.
Key words: norovirus / neoglycoprotein / secretor / sialyl Lewis x / virus-like particle
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