ArticlePLoS pathogens2020
Dynamic rotation of the protruding domain enhances the infectivity of norovirus.
Article in PLoS pathogens, 2020. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 48 citations in OpenAlex.
- Symmetry-breaking antibody binding reveals extensive capsid malleability in pandemic human norovirus.Research square · 2026Article
- Serum IgA proteomics reveals clonal composition and neutralization of dimeric and monomeric IgA repertoires against human norovirus.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- 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
- Bridging the Structural Gap: A Methodological Review of Cryo-Electron Microscopy for Underrepresented Viruses.Viruses · 2026Review
- 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
- Norovirus replication, host interactions and vaccine advances.Nature reviews. Microbiology · 2025Review
- 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
- Molecular Mechanism of pH-Induced Protrusion Configuration Switching in Piscine Betanodavirus Implies a Novel Antiviral Strategy.ACS infectious diseases · 2024Article
- Bacillaceae serine proteases and Streptomyces epsilon-poly-L-lysine synergistically inactivate Caliciviridae by inhibiting RNA genome release.Scientific reports · 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
- Production of infectious reporter murine norovirus by VP2Journal of virology · 2024Article
- A single nanobody neutralizes multiple epochally evolving human noroviruses by modulating capsid plasticity.Nature communications · 2023Article
- Article
- CLIC and membrane wound repair pathways enable pandemic norovirus entry and infection.Nature communications · 2023Article
- Functional and structural characterization of Norovirus GII.6 in recognizing histo-blood group antigens.Virologica Sinica · 2023Article
- Structural Basis for Rabbit Hemorrhagic Disease Virus Antibody Specificity.Journal of virology · 2022Article
- Distinct dissociation rates of murine and human norovirus P-domain dimers suggest a role of dimer stability in virus-host interactions.Communications biology · 2022Article
- Atomic Structure of the Human Sapovirus Capsid Reveals a Unique Capsid Protein Conformation in Caliciviruses.Journal of virology · 2022Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Norovirus is the major cause of epidemic nonbacterial gastroenteritis worldwide. Lack of structural information on infection and replication mechanisms hampers the development of effective vaccines and remedies. Here, using cryo-electron microscopy, we show that the capsid structure of murine noroviruses changes in response to aqueous conditions. By twisting the flexible hinge connecting two domains, the protruding (P) domain reversibly rises off the shell (S) domain in solutions of higher pH, but rests on the S domain in solutions of lower pH. Metal ions help to stabilize the resting conformation in this process. Furthermore, in the resting conformation, the cellular receptor CD300lf is readily accessible, and thus infection efficiency is significantly enhanced. Two similar P domain conformations were also found simultaneously in the human norovirus GII.3 capsid, although the mechanism of the conformational change is not yet clear. These results provide new insights into the mechanisms of non-enveloped norovirus transmission that invades host cells, replicates, and sometimes escapes the hosts immune system, through dramatic environmental changes in the gastrointestinal tract.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.