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10:46
Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography
Published on: April 19, 2016
Human noroviruses recognize sialyl Lewis x neoglycoprotein
Gustaf E Rydell1, Jonas Nilsson, Jesus Rodriguez-Diaz
1Department of Clinical Chemistry and Transfusion Medicine, Sahlgrenska University Hospital, Göteborg, Sweden.
Glycobiology
|December 5, 2008
Summary
Norovirus GII strains bind to specific carbohydrates, including sialyl Lewis x, which is a novel finding. This dual binding specificity influences norovirus infection and transmission pathways.
Area of Science:
- Virology
- Carbohydrate Chemistry
- Immunology
Background:
- Norovirus GII strains are a significant cause of human gastroenteritis.
- Understanding norovirus-carbohydrate interactions is crucial for developing prevention strategies.
Purpose of the Study:
- To investigate the carbohydrate binding characteristics of norovirus GII.3 and GII.4 strains.
- To identify specific carbohydrate structures recognized by these norovirus strains.
Main Methods:
- Utilized virus-like particles (VLPs) of norovirus GII.3 and GII.4 strains.
- Analyzed binding to saliva samples from individuals with known secretor and Lewis blood group genotypes.
- Assayed binding to various neoglycoproteins and characterized minimal binding requirements.
Main Results:
- Norovirus GII VLPs exhibited secretor-gene-dependent binding, with stronger affinity for A, B, and AB blood group individuals.
- Both GII.3 and GII.4 strains demonstrated specific binding to sialyl Lewis x, a novel finding.
- Sialyl Lewis x conjugates were potent inhibitors of VLP binding, indicating its importance as a receptor structure.
Conclusions:
- Human norovirus GII strains possess at least two distinct binding specificities.
- These specificities include secretor-gene-dependent binding to alpha1,2-fucosylated carbohydrates and binding to alpha2,3-sialylated carbohydrates like sialyl Lewis x.
- This dual binding capability likely contributes to norovirus infectivity and host range.
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