ArticlePLoS biology2020
Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM.
Article in PLoS biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- 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
- A VLP vaccine platform comprising the core protein of hepatitis B virus with N-terminal antigen capture.International journal of biological macromolecules · 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
- Mechanism of enterovirus VP0 maturation cleavage based on the structure of a stabilised assembly intermediate.PLoS pathogens · 2024Article
- Mechanism of enterovirus VP0 maturation cleavage based on the structure of a stabilised assembly intermediate.bioRxiv : the preprint server for biology · 2024Article
- Amino acid substitutions in norovirus VP1 dictate host dissemination via variations in cellular attachment.Journal of virology · 2023Article
- Article
- 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
- Atomic structure of the predominant GII.4 human norovirus capsid reveals novel stability and plasticity.Nature communications · 2022Article
- Determination of murine norovirus aerosol concentration during toilet flushing.Scientific reports · 2021Article
- Review
- Multiple Signals in the Gut Contract the Mouse Norovirus Capsid To Block Antibody Binding While Enhancing Receptor Affinity.Journal of virology · 2021Article
- Review
- Exploring the Effect of Structure-Based Scaffold Hopping on the Inhibition of Coxsackievirus A24v Transduction by Pentavalent N-Acetylneuraminic Acid Conjugates.International journal of molecular sciences · 2021Article
- Norovirus evolution in immunodeficient mice reveals potentiated pathogenicity via a single nucleotide change in the viral capsid.PLoS pathogens · 2021Article
- Cryo-EM structures reveal two distinct conformational states in a picornavirus cell entry intermediate.PLoS pathogens · 2020Article
- Dynamic rotation of the protruding domain enhances the infectivity of norovirus.PLoS pathogens · 2020Article
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Authors and funding
6 authors.
Funding
Abstract
Icosahedral viral capsids must undergo conformational rearrangements to coordinate essential processes during the viral life cycle. Capturing such conformational flexibility has been technically challenging yet could be key for developing rational therapeutic agents to combat infections. Noroviruses are nonenveloped, icosahedral viruses of global importance to human health. They are a common cause of acute gastroenteritis, yet no vaccines or specific antiviral agents are available. Here, we use genetics and cryo-electron microscopy (cryo-EM) to study the high-resolution solution structures of murine norovirus as a model for human viruses. By comparing our 3 structures (at 2.9- to 3.1-Å resolution), we show that whilst there is little change to the shell domain of the capsid, the radiating protruding domains are flexible, adopting distinct states both independently and synchronously. In doing so, the capsids sample a range of conformational space, with implications for maintaining virion stability and infectivity.
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Registered trials
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