ArticleJournal of virology2006
Assembly of highly infectious rotavirus particles recoated with recombinant outer capsid proteins.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed.
- Mechanism of membrane perforation in rotavirus cell entry.bioRxiv : the preprint server for biology · 2026Article
- Structural determinants of rotavirus proteolytic activation.PLoS pathogens · 2025Article
- The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to Ca2.PLoS pathogens · 2024Article
- Review
- Rotavirus Spike Protein VP4 Mediates Viroplasm Assembly by Association to Actin Filaments.Journal of virology · 2022Article
- Using Species a Rotavirus Reverse Genetics to Engineer Chimeric Viruses Expressing SARS-CoV-2 Spike Epitopes.Journal of virology · 2022Article
- Investigation of Pathogenic Mechanism of Covert Mortality Nodavirus Infection inFrontiers in microbiology · 2022Article
- Recent advances in rotavirus reverse genetics and its utilization in basic research and vaccine development.Archives of virology · 2021Review
- Reverse genetic engineering of simian rotaviruses with temperature-sensitive lesions in VP1, VP2, and VP6.Virus research · 2021Article
- Review
- Article
- Understanding the penetrance of intrinsic protein disorder in rotavirus proteome.International journal of biological macromolecules · 2020Article
- Article
- The C Terminus of Rotavirus VP4 Protein Contains an Actin Binding Domain Which Requires Cooperation with the Coiled-Coil Domain for Actin Remodeling.Journal of virology · 2019Article
- Visualization of Calcium Ion Loss from Rotavirus during Cell Entry.Journal of virology · 2018Article
- Article
- 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
- Inflammatory and oxidative stress in rotavirus infection.World journal of virology · 2016Review
- Structural correlates of rotavirus cell entry.PLoS pathogens · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Assembly of the rotavirus outer capsid is the final step of a complex pathway. In vivo, the later steps include a maturational membrane penetration that is dependent on the scaffolding activity of a viral nonstructural protein. In vitro, simply adding the recombinant outer capsid proteins VP4 and VP7 to authentic double-layered rotavirus subviral particles (DLPs) in the presence of calcium and acidic pH increases infectivity by a factor of up to 10(7), yielding particles as infectious as authentic purified virions. VP4 must be added before VP7 for high-level infectivity. Steep dependence of infectious recoating on VP4 concentration suggests that VP4-VP4 interactions, probably oligomerization, precede VP4 binding to particles. Trypsin sensitivity analysis identifies two populations of VP4 associated with recoated particles: properly mounted VP4 that can be specifically primed by trypsin, and nonspecifically associated VP4 that is degraded by trypsin. A full complement of properly assembled VP4 is not required for efficient infectivity. Minimal dependence of recoating on VP7 concentration suggests that VP7 binds DLPs with high affinity. The parameters for efficient recoating and the characterization of recoated particles suggest a model in which, after a relatively weak interaction between oligomeric VP4 and DLPs, VP7 binds the particles and locks VP4 in place. Recoating will allow the use of infectious modified rotavirus particles to explore rotavirus assembly and cell entry and could lead to practical applications in novel immunization strategies.
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Registered trials
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