ArticleJournal of virology2018
Atomic Structure of the Murine Norovirus Protruding Domain and Soluble CD300lf Receptor Complex.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- Murine norovirus allosteric escape mutants mimic gut activation.Journal of virology · 2025Article
- TREM-1 as a Potential Coreceptor in Norovirus Pathogenesis: Insights from Transcriptomic Analysis and Molecular Docking.ACS omega · 2025Article
- Current trends and new approaches for human norovirus replication in cell culture: a literature review.Archives of virology · 2024Review
- The reversible activation of norovirus by metal ions.Journal of virology · 2024Article
- Genetic diversity of murine norovirus populations less susceptible to chlorine.Frontiers in microbiology · 2024Article
- Amino acid substitutions in norovirus VP1 dictate host dissemination via variations in cellular attachment.Journal of virology · 2023Article
- 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
- Human Noroviruses Attach to Intestinal Tissues of a Broad Range of Animal Species.Journal of virology · 2021Article
- Inhibitory Effects ofViruses · 2020Article
- 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
- 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
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human noroviruses are the leading cause of acute gastroenteritis in humans. Noroviruses also infect animals, such as cows, mice, cats, and dogs. How noroviruses bind and enter host cells is still incompletely understood. Recently, the type I transmembrane protein CD300lf was identified as the murine norovirus receptor, yet it is unclear how the virus capsid and receptor interact at the molecular level. In this study, we determined the X-ray crystal structure of the soluble CD300lf (sCD300lf) and the murine norovirus capsid protruding domain complex at a 2.05-Å resolution. We found that the sCD300lf-binding site is located on the topside of the protruding domain and involves a network of hydrophilic and hydrophobic interactions. sCD300lf locked nicely into a complementary cavity on the protruding domain that is additionally coordinated with a positive surface charge on sCD300lf and a negative surface charge on the protruding domain. Five of six protruding domain residues interacting with sCD300lf were maintained between different murine norovirus strains, suggesting that sCD300lf was capable of binding to a highly conserved pocket. Moreover, a sequence alignment with other CD300 paralogs showed that the sCD300lf-interacting residues were partially conserved in CD300ld but variable in other CD300 family members, consistent with previously reported infection selectivity. Overall, these data provide insights into how a norovirus engages a protein receptor and will be important for a better understanding of selective recognition and norovirus attachment and entry mechanisms.
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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.