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Norovirus Escape from Broadly Neutralizing Antibodies Is Limited to Allostery-Like Mechanisms.
Article in mSphere. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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Who cites it
30 citing papers in PubMed, 37 citations in OpenAlex.
- Molecular Characterization and Epidemiology of Human Noroviruses in the Sverdlovsk Region, Russian Federation.Viruses · 2025Article
- Murine norovirus allosteric escape mutants mimic gut activation.Journal of virology · 2025Article
- Conformational Flexibility in Capsids Encoded by theViruses · 2024Review
- Mouse and human immune responses share neutralization epitopes of HAstV-VA1.Journal of virology · 2024Article
- The reversible activation of norovirus by metal ions.Journal of virology · 2024Article
- Broad-Spectrum, Potent, and Durable Ceria Nanoparticles Inactivate RNA Virus Infectivity by Targeting Virion Surfaces and Disrupting Virus-Receptor Interactions.Molecules (Basel, Switzerland) · 2023Article
- Epidemiology and genetic diversity of norovirus GII genogroups among children in Hubei, China, 2017-2019.Virologica Sinica · 2023Article
- Mouse Norovirus Uses Host Metabolites to Enhance Receptor Binding and Evade Immune Recognition.Medical research archives · 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
- Insights on the mutational landscape of the SARS-CoV-2 Omicron variant receptor-binding domain.Cell reports. Medicine · 2022Article
- Multiple Signals in the Gut Contract the Mouse Norovirus Capsid To Block Antibody Binding While Enhancing Receptor Affinity.Journal of virology · 2021Article
- Review
- A Norovirus Uses Bile Salts To Escape Antibody Recognition While Enhancing Receptor Binding.Journal of virology · 2021Article
- Article
- Nanobody-Mediated Neutralization Reveals an Achilles Heel for Norovirus.Journal of virology · 2020Article
- The Dynamic Life of Virus Capsids.Viruses · 2020Review
- Precise location of linear epitopes on the capsid surface of feline calicivirus recognized by neutralizing and non-neutralizing monoclonal antibodies.Veterinary research · 2020Article
- CD300lf is the primary physiologic receptor of murine norovirus but not human norovirus.PLoS pathogens · 2020Article
- Bile Salts Alter the Mouse Norovirus Capsid Conformation: Possible Implications for Cell Attachment and Immune Evasion.Journal of virology · 2019Article
- Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Ideal antiviral vaccines elicit antibodies (Abs) with broad strain recognition that bind to regions that are difficult to mutate for escape. Using 10 murine norovirus (MNV) strains and 5 human norovirus (HuNoV) virus-like particles (VLPs), we identified monoclonal antibody (MAb) 2D3, which broadly neutralized all MNV strains tested. Importantly, escape mutants corresponding to this antibody were very slow to develop and were distal to those raised against our previously studied antibody, A6.2. To understand the atomic details of 2D3 neutralization, we determined the cryo-electron microscopy (cryo-EM) structure of the 2D3/MNV1 complex. Interestingly, 2D3 binds to the top of the P domain, very close to where A6.2 binds, but the only escape mutations identified to date fall well outside the contact regions of both 2D3 and A6.2. To determine how mutations in distal residues could block antibody binding, we used molecular dynamics flexible fitting simulations of the atomic structures placed into the density map to examine the 2D3/MNV1 complex and these mutations. Our findings suggest that the escape mutant, V339I, may stabilize a salt bridge network at the P-domain dimer interface that, in an allostery-like manner, affects the conformational relaxation of the P domain and the efficiency of binding. They further highlight the unusual antigenic surface bound by MAb 2D3, one which elicits cross-reactive antibodies but which the virus is unable to alter to escape neutralization. These results may be leveraged to generate norovirus (NoV) vaccines containing broadly neutralizing antibodies.
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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.