ArticleJournal of virology2010
High-resolution x-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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
53 citing papers in PubMed, 88 citations in OpenAlex.
- Bile acids accumulate norovirus-like particles and enhance binding to and entry into human enteric epithelial cells.Journal of virology · 2026Article
- Murine norovirus allosteric escape mutants mimic gut activation.Journal of virology · 2025Article
- The reversible activation of norovirus by metal ions.Journal of virology · 2024Article
- Characterization of surface-exposed structural loops as insertion sites for foreign antigen delivery in calicivirus-derived VLP platform.Frontiers in microbiology · 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
- Assignment of Ala, Ile, LeuBiomolecular NMR assignments · 2022Article
- Environmentally-triggered contraction of the norovirus virion determines diarrheagenic potential.Frontiers in immunology · 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
- NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins.Viruses · 2021Article
- Dynamic rotation of the protruding domain enhances the infectivity of norovirus.PLoS pathogens · 2020Article
- Nanobody-Mediated Neutralization Reveals an Achilles Heel for Norovirus.Journal of virology · 2020Article
- The Dynamic Life of Virus Capsids.Viruses · 2020Review
- Impact of pH and protein hydrophobicity on norovirus inactivation by heat-denatured lysozyme.PloS one · 2020Article
- Bile Salts Alter the Mouse Norovirus Capsid Conformation: Possible Implications for Cell Attachment and Immune Evasion.Journal of virology · 2019Article
- Norovirus Attachment and Entry.Viruses · 2019Review
- Review
- The Dynamic Capsid Structures of the Noroviruses.Viruses · 2019Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Murine noroviruses (MNV) are closely related to the human noroviruses (HuNoV), which cause the majority of nonbacterial gastroenteritis. Unlike HuNoV, MNV grow in culture and in a small-animal model that represents a tractable model to study norovirus biology. To begin a detailed investigation of molecular events that occur during norovirus binding to cells, the crystallographic structure of the murine norovirus 1 (MNV-1) capsid protein protruding (P) domain has been determined. Crystallization of the bacterially expressed protein yielded two different crystal forms (Protein Data Bank identifiers [PDB ID], 3LQ6 and 3LQE). Comparison of the structures indicated a large degree of structural mobility in loops on the surface of the P2 subdomain. Specifically, the A'-B' and E'-F' loops were found in open and closed conformations. These regions of high mobility include the known escape mutation site for the neutralizing antibody A6.2 and an attenuation mutation site, which arose after serial passaging in culture and led to a loss in lethality in STAT1(-/-) mice, respectively. Modeling of a Fab fragment and crystal structures of the P dimer into the cryoelectron microscopy three-dimensional (3D) image reconstruction of the A6.2/MNV-1 complex indicated that the closed conformation is most likely bound to the Fab fragment and that the antibody contact is localized to the A'-B' and E'-F' loops. Therefore, we hypothesize that these loop regions and the flexibility of the P domains play important roles during MNV-1 binding to the cell surface.
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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.