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Human noroviruses r...
Human noroviruses recognize sialyl Lewis x neoglycoprotein
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- Rydell, Gustaf E (författare)
- Sahlgrens University Hospital
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- Nilsson, Jonas (författare)
- Sahlgrens University Hospital
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- Rodriguez, Jesus (författare)
- Linköpings universitet,Hälsouniversitetet,Molekylär virologi
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- Ruvoen-Clouet, Nathalie (författare)
- INSERM
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- Svensson, Lennart (författare)
- Linköpings universitet,Molekylär virologi,Hälsouniversitetet
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- Le Pendu, Jacques (författare)
- INSERM
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- Larson, Goran (författare)
- Sahlgrens University Hospital
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(creator_code:org_t)
- 2008-12-03
- 2009
- Engelska.
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Ingår i: Glycobiology. - : Oxford University Press (OUP). - 0959-6658 .- 1460-2423. ; 19:3, s. 309-320
- Relaterad länk:
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https://academic.oup...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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 A(2) 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 alpha 3Gal beta 4(Fuc alpha 3)GlcNAc beta 3Gal beta- 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 alpha 1,2-fucosylated carbohydrates and another related to alpha 2,3-sialylated carbohydrates of the type 2 chain, e.g., sialyl Lewis x.
Nyckelord
- norovirus
- neoglycoprotein
- secretor
- sialyl Lewis x
- virus-like particle
- MEDICINE
- MEDICIN
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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