ArticleChembiochem : a European journal of chemical biology2020
Chemical-Shift Perturbations Reflect Bile Acid Binding to Norovirus Coat Protein: Recognition Comes in Different Flavors.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 21 citations in OpenAlex.
- Bile acids accumulate norovirus-like particles and enhance binding to and entry into human enteric epithelial cells.Journal of virology · 2026Article
- Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Conformational Flexibility in Capsids Encoded by theViruses · 2024Review
- Metabolic immaturity and breastmilk bile acid metabolites are central determinants of heightened newborn vulnerability to norovirus diarrhea.Cell host & microbe · 2024Article
- Conformational Control of Fast Asparagine Deamidation in a Norovirus Capsid Protein.Biochemistry · 2023Article
- Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Distinct dissociation rates of murine and human norovirus P-domain dimers suggest a role of dimer stability in virus-host interactions.Communications biology · 2022Article
- Glycan Recognition in Human Norovirus Infections.Viruses · 2021Review
- Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses.Nature communications · 2021Article
- Protein Secondary Structure Affects Glycan Clustering in Native Mass Spectrometry.Life (Basel, Switzerland) · 2021Article
- Bile Goes Viral.Viruses · 2021Review
- NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins.Viruses · 2021Article
- Chemical-Shift Perturbations Reflect Bile Acid Binding to Norovirus Coat Protein: Recognition Comes in Different Flavors.Chembiochem : a European journal of chemical biology · 2020Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bile acids have been reported as important cofactors promoting human and murine norovirus (NoV) infections in cell culture. The underlying mechanisms are not resolved. Through the use of chemical shift perturbation (CSP) NMR experiments, we identified a low-affinity bile acid binding site of a human GII.4 NoV strain. Long-timescale MD simulations reveal the formation of a ligand-accessible binding pocket of flexible shape, allowing the formation of stable viral coat protein-bile acid complexes in agreement with experimental CSP data. CSP NMR experiments also show that this mode of bile acid binding has a minor influence on the binding of histo-blood group antigens and vice versa. STD NMR experiments probing the binding of bile acids to virus-like particles of seven different strains suggest that low-affinity bile acid binding is a common feature of human NoV and should therefore be important for understanding the role of bile acids as cofactors in NoV infection.
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