ArticleNature communications2022
Atomic structure of the predominant GII.4 human norovirus capsid reveals novel stability and plasticity.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 52 citations in OpenAlex.
- Cross-Neutralizing and Broadly Neutralizing Human Antibodies Against Nonenveloped Viruses.European journal of immunology · 2026Review
- Conformational Plasticity of the Human Norovirus GII.3 Capsid Reveals Alternative P Domain Interaction Networks.International journal of molecular sciences · 2026Article
- Balancing under constraint: Structural insights into norovirus evolution and antigenic innovation.PLoS pathogens · 2026Article
- A Prolonged Norovirus Infection and the Molecular Evolution of Human Norovirus Within-Host in a Child with Burkitt Lymphoma.Viruses · 2026Article
- Variable and conserved B cell epitopes of GII.4 human noroviruses.Journal of virology · 2026Review
- Mutational analysis of human norovirus VP2 elucidates critical molecular interactions for virus assembly.Journal of virology · 2026Article
- Calicivirus assembly and stability are mediated by the N-terminal domain of the capsid protein with the involvement of the viral genome.PLoS pathogens · 2025Article
- Functional diversity in GII.4 norovirus entry: HBGA binding and capsid clustering dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Murine norovirus allosteric escape mutants mimic gut activation.Journal of virology · 2025Article
- Norovirus replication, host interactions and vaccine advances.Nature reviews. Microbiology · 2025Review
- Article
- Structural and stability differences among GI norovirus virus-like particles produced in silkworm-baculovirus expression vector system.Frontiers in microbiology · 2025Article
- Conformational Flexibility in Capsids Encoded by theViruses · 2024Review
- Near-atomic structures of RHDV reveal insights into capsid assembly and different conformations between mature virion and VLP.Journal of virology · 2024Article
- Human norovirus disturbs intestinal motility and transit time through its capsid proteins.PLoS pathogens · 2024Article
- Molecular Mechanism of pH-Induced Protrusion Configuration Switching in Piscine Betanodavirus Implies a Novel Antiviral Strategy.ACS infectious diseases · 2024Article
- Structural analyses of the GI.4 norovirus by cryo-electron microscopy and X-ray crystallography revealing binding sites for human monoclonal antibodies.Journal of virology · 2024Article
- Molecular Evolution of GII.P31/GII.4_Sydney_2012 Norovirus over a Decade in a Clinic in Japan.International journal of molecular sciences · 2024Article
- Article
- The reversible activation of norovirus by metal ions.Journal of virology · 2024Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Human noroviruses (HuNoVs) cause sporadic and epidemic viral gastroenteritis worldwide. The GII.4 variants are responsible for most HuNoV infections, and GII.4 virus-like particles (VLPs) are being used in vaccine development. The atomic structure of the GII.4 capsid in the native T = 3 state has not been determined. Here we present the GII.4 VLP structure with T = 3 symmetry determined using X-ray crystallography and cryo-EM at 3.0 Å and 3.8 Å resolution, respectively, which reveals unanticipated novel features. A novel aspect in the crystal structure determined without imposing icosahedral symmetry is the remarkable adaptability of the capsid protein VP1 driven by the flexible hinge between the shell and the protruding domains. In both crystal and cryo-EM structures, VP1 adopts a stable conformation with the protruding domain resting on the shell domain, in contrast to the 'rising' conformation observed in recent cryo-EM structures of other GII.4 VLPs. Our studies further revealed that the resting state of VP1 dimer is stabilized by a divalent ion, and chelation using EDTA increases capsid diameter, exposing new hydrophobic and antigenic sites and suggesting a transition to the rising conformation. These novel insights into GII.4 capsid structure, stability, and antigen presentation may be useful for ongoing vaccine development.
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