ArticleJournal of virology2010
Conformational changes in the capsid of a calicivirus upon interaction with its functional receptor.
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 41 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
41 citing papers in PubMed, 76 citations in OpenAlex.
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- Unlocking the secrets of Feline calicivirus: advances in structural and nonstructural proteins and its role as a key model for other Caliciviruses.Virology journal · 2025Review
- Epitope mapping of a neutralizing antibody against rabbit hemorrhagic disease virus GI.2.Veterinary research · 2025Article
- Isolation, Identification, and Genetic Evolution Analysis ofInternational journal of molecular sciences · 2025Article
- Analysis of Genetic Diversity Based on Sequences of Feline Calicivirus Strains Isolated in China.Transboundary and emerging diseases · 2025Article
- Conformational Flexibility in Capsids Encoded by theViruses · 2024Review
- Screening and Immune Efficacy Evaluation of Antigens with Protection Against Feline Calicivirus.Vaccines · 2024Article
- VP2 mediates the release of the feline calicivirus RNA genome by puncturing the endosome membrane of infected cells.Journal of virology · 2024Article
- Biological Characteristics of Feline Calicivirus Epidemic Strains in China and Screening of Broad-Spectrum Protective Vaccine Strains.Vaccines · 2023Article
- A single nanobody neutralizes multiple epochally evolving human noroviruses by modulating capsid plasticity.Nature communications · 2023Article
- Efficacy of EPA-registered disinfectants against two human norovirus surrogates and Clostridioides difficile endospores.Journal of applied microbiology · 2022Article
- Atomic Structure of the Human Sapovirus Capsid Reveals a Unique Capsid Protein Conformation in Caliciviruses.Journal of virology · 2022Article
- Atomic structure of the predominant GII.4 human norovirus capsid reveals novel stability and plasticity.Nature communications · 2022Article
- Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses.Nature communications · 2021Article
- The Cryo-EM Structure of Vesivirus 2117 Highlights Functional Variations in Entry Pathways for Viruses in Different Clades of theJournal of virology · 2021Article
- A De novo Peptide from a High Throughput Peptide Library Blocks Myosin A -MTIP Complex Formation inInternational journal of molecular sciences · 2020Article
- Article
- Dynamic rotation of the protruding domain enhances the infectivity of norovirus.PLoS pathogens · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Nonenveloped viral capsids are metastable structures that undergo conformational changes during virus entry that lead to interactions of the capsid or capsid fragments with the cell membrane. For members of the Caliciviridae, neither the nature of these structural changes in the capsid nor the factor(s) responsible for inducing these changes is known. Feline junctional adhesion molecule A (fJAM-A) mediates the attachment and infectious viral entry of feline calicivirus (FCV). Here, we show that the infectivity of some FCV isolates is neutralized following incubation with the soluble receptor at 37 degrees C. We used this property to select mutants resistant to preincubation with the soluble receptor. We isolated and sequenced 24 soluble receptor-resistant (srr) mutants and characterized the growth properties and receptor-binding activities of eight mutants. The location of the mutations within the capsid structure of FCV was mapped using a new 3.6-A structure of native FCV. The srr mutations mapped to the surface of the P2 domain were buried at the protruding domain dimer interface or were present in inaccessible regions of the capsid protein. Coupled with data showing that both the parental FCV and the srr mutants underwent increases in hydrophobicity upon incubation with the soluble receptor at 37 degrees C, these findings indicate that FCV likely undergoes conformational change upon interaction with its receptor. Changes in FCV capsid conformation following its interaction with fJAM-A may be important for subsequent interactions of the capsid with cellular membranes, membrane penetration, and genome delivery.
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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.