ArticleJournal of virology2012
Structural basis for broad detection of genogroup II noroviruses by a monoclonal antibody that binds to a site occluded in the viral particle.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
62 citing papers in PubMed, 86 citations in OpenAlex.
- Symmetry-breaking antibody binding reveals extensive capsid malleability in pandemic human norovirus.Research square · 2026Article
- Variable and conserved B cell epitopes of GII.4 human noroviruses.Journal of virology · 2026Review
- Highly variable antigenic site located at the apex of GII.4 norovirus capsid protein induces cross-reactive blocking antibodies in a variant-specific manner.Journal of virology · 2025Article
- Manipulation of immunodominant variable epitopes of norovirus capsid protein elicited cross-blocking antibodies to different GII.4 variants despite the low potency of the polyclonal sera.Journal of virology · 2025Article
- Murine norovirus allosteric escape mutants mimic gut activation.Journal of virology · 2025Article
- Conformational Flexibility in Capsids Encoded by theViruses · 2024Review
- 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
- The reversible activation of norovirus by metal ions.Journal of virology · 2024Article
- A single nanobody neutralizes multiple epochally evolving human noroviruses by modulating capsid plasticity.Nature communications · 2023Article
- Article
- Structural Basis for Rabbit Hemorrhagic Disease Virus Antibody Specificity.Journal of virology · 2022Article
- Mouse Norovirus Uses Host Metabolites to Enhance Receptor Binding and Evade Immune Recognition.Medical research archives · 2022Article
- Development of a Specific Anti-capsid Antibody- and Magnetic Bead-Based Immunoassay to Detect Human Norovirus Particles in Stool Samples and Spiked Mussels via Flow Cytometry.Food and environmental virology · 2021Article
- A luciferase-based approach for measuring HBGA blockade antibody titers against human norovirus.Journal of virological methods · 2021Article
- Multiple Signals in the Gut Contract the Mouse Norovirus Capsid To Block Antibody Binding While Enhancing Receptor Affinity.Journal of virology · 2021Article
- Review
- Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses.Nature communications · 2021Article
- A Norovirus Uses Bile Salts To Escape Antibody Recognition While Enhancing Receptor Binding.Journal of virology · 2021Article
- Disulfide stabilization of human norovirus GI.1 virus-like particles focuses immune response toward blockade epitopes.NPJ vaccines · 2020Article
- Dynamic rotation of the protruding domain enhances the infectivity of norovirus.PLoS pathogens · 2020Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 6 institutions in 2 countries.
Funding
Abstract
Human noroviruses are genetically and antigenically highly divergent. Monoclonal antibodies raised in mice against one kind of norovirus virus-like particle (VLP), however, were found to have broad recognition. In this study, we present the crystal structure of the antigen-binding fragment (Fab) for one of these broadly reactive monoclonal antibodies, 5B18, in complex with the capsid-protruding domain from a genogroup II genotype 10 (GII.10) norovirus at 3.3-Å resolution and, also, the cryo-electron microscopy structure of the GII.10 VLP at ∼10-Å resolution. The GII.10 VLP structure was more similar in overall architecture to the GV.1 murine norovirus virion than to the prototype GI.1 human norovirus VLP, with the GII.10 protruding domain raised ∼15 Å off the shell domain and rotated ∼40° relative to the GI.1 protruding domain. In the crystal structure, the 5B18 Fab bound to a highly conserved region of the protruding domain. Based on the VLP structure, this region is involved in interactions with other regions of the capsid and is buried in the virus particle. Despite the occluded nature of the recognized epitope in the VLP structure, enzyme-linked immunosorbent assay (ELISA) binding suggested that the 5B18 antibody was able to capture intact VLPs. Together, the results provide evidence that the norovirus particle is capable of extreme conformational flexibility, which may allow for antibody recognition of conserved surfaces that would otherwise be buried on intact particles.
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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.