ArticleJournal of virology2010
Effect of mutations in VP5 hydrophobic loops on rotavirus cell entry.
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 31 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
31 citing papers in PubMed.
- Whole-genome characterization and phylogenetic analysis of Equine Rotavirus A isolated from Jeju Island, Korea.Journal of veterinary science · 2026Article
- Review
- Mutations of two amino acids in VP5 mediate the attenuation of human rotavirus vaccine: evidence fromJournal of virology · 2025Article
- Human Rotaviruses of Multiple Genotypes Acquire Conserved VP4 Mutations during Serial Passage.Viruses · 2024Article
- The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to Ca2.PLoS pathogens · 2024Article
- Review
- The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to CabioRxiv : the preprint server for biology · 2023Article
- Using Species a Rotavirus Reverse Genetics to Engineer Chimeric Viruses Expressing SARS-CoV-2 Spike Epitopes.Journal of virology · 2022Article
- Article
- Control of Capsid Transformations during Reovirus Entry.Viruses · 2021Review
- Infection of porcine small intestinal enteroids with human and pig rotavirus A strains reveals contrasting roles for histo-blood group antigens and terminal sialic acids.PLoS pathogens · 2021Article
- Article
- The Arginines in the N-Terminus of the Porcine Circovirus 2 Virus-like Particles Are Responsible for Disrupting the Membranes at Neutral and Acidic pH.Journal of molecular biology · 2019Article
- Detection of Norovirus and Rotavirus Present in Suspended and Dissolved Forms in Drinking Water Sources.Food and environmental virology · 2019Article
- Visualization of Calcium Ion Loss from Rotavirus during Cell Entry.Journal of virology · 2018Article
- Virus Type-Specific Removal in a Full-Scale Membrane Bioreactor Treatment Process.Food and environmental virology · 2018Article
- Single-Particle Detection of Transcription following Rotavirus Entry.Journal of virology · 2017Article
- Identification and characterization of vp7 gene in Bombyx mori cytoplasmic polyhedrosis virus.Gene · 2017Article
- Mechanism of membrane fusion induced by vesicular stomatitis virus G protein.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Carbohydrate recognition by rotaviruses.Journal of structural and functional genomics · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Experiments in cell-free systems have demonstrated that the VP5 cleavage fragment of the rotavirus spike protein, VP4, undergoes a foldback rearrangement that translocates three clustered hydrophobic loops from one end of the molecule to the other. This conformational change resembles the foldback rearrangements of enveloped virus fusion proteins. By recoating rotavirus subviral particles with recombinant VP4 and VP7, we tested the effects on cell entry of substituting hydrophilic for hydrophobic residues in the clustered VP5 loops. Several of these mutations decreased the infectivity of recoated particles without preventing either recoating or folding back. In particular, the V391D mutant had a diminished capacity to interact with liposomes when triggered to fold back by serial protease digestion in solution, and particles recoated with this mutant VP4 were 10,000-fold less infectious than particles recoated with wild-type VP4. Particles with V391D mutant VP4 attached normally to cells and internalized efficiently, but they failed in the permeabilization step that allows coentry of the toxin alpha-sarcin. These findings indicate that the hydrophobicity of the VP5 apex is required for membrane disruption during rotavirus cell entry.
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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.