ArticleViruses2021
NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins.
Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Internalization and Localization of Murine Norovirus in Hydroponically Grown Green Onion (Allium Fistulosum L.).Food and environmental virology · 2026Article
- Atomic force microscopy at the forefront: unveiling foodborne viruses with biophysical tools.Npj viruses · 2025Review
- Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Conformational Control of Fast Asparagine Deamidation in a Norovirus Capsid Protein.Biochemistry · 2023Article
- Exploring multivalent carbohydrate-protein interactions by NMR.Chemical Society reviews · 2023Review
- Assignment of Ala, Ile, LeuBiomolecular NMR assignments · 2022Article
- Norovirus-glycan interactions - how strong are they really?Biochemical Society transactions · 2022Article
- Review
- Review
- Glycan Recognition in Human Norovirus Infections.Viruses · 2021Review
- Characterization of Functional Components in Bovine Colostrum That Inhibit Norovirus Capsid Protruding Domains Interacting with HBGA Ligands.Pathogens (Basel, Switzerland) · 2021Article
- Protein Secondary Structure Affects Glycan Clustering in Native Mass Spectrometry.Life (Basel, Switzerland) · 2021Article
- Glycan-Induced Protein Dynamics in Human Norovirus P Dimers Depend on Virus Strain and Deamidation Status.Molecules (Basel, Switzerland) · 2021Article
- Quantifying Protein-Glycan Interactions Using Native Mass Spectrometry.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycan-protein interactions are highly specific yet transient, rendering glycans ideal recognition signals in a variety of biological processes. In human norovirus (HuNoV) infection, histo-blood group antigens (HBGAs) play an essential but poorly understood role. For murine norovirus infection (MNV), sialylated glycolipids or glycoproteins appear to be important. It has also been suggested that HuNoV capsid proteins bind to sialylated ganglioside head groups. Here, we study the binding of HBGAs and sialoglycans to HuNoV and MNV capsid proteins using NMR experiments. Surprisingly, the experiments show that none of the norovirus P-domains bind to sialoglycans. Notably, MNV P-domains do not bind to any of the glycans studied, and MNV-1 infection of cells deficient in surface sialoglycans shows no significant difference compared to cells expressing respective glycans. These findings redefine glycan recognition by noroviruses, challenging present models of infection.
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Registered trials
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