ArticleJournal of virology2012
In vitro assembly of an empty picornavirus capsid follows a dodecahedral path.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed.
- N-terminal truncation of the foot-and-mouth disease virus VP0 protein promotes soluble co-expression and particle assembly stability of viral capsid proteins in Escherichia coli.BMC biotechnology · 2025Article
- Some assembly required: a single-RNA vaccine against enterovirus-D68.Trends in pharmacological sciences · 2024Article
- Structural Insights into Common and Host-Specific Receptor-Binding Mechanisms in Algal Picorna-like Viruses.Viruses · 2022Article
- Pathological Features of Echovirus-11-Associated Brain Damage in Mice Based on RNA-Seq Analysis.Viruses · 2021Article
- Mechanisms for destabilisation of RNA viruses at air-water and liquid-liquid interfaces.Nature communications · 2021Article
- Review
- An Engineered Maturation Cleavage Provides a Recombinant Mimic of Foot-and-Mouth Disease Virus Capsid Assembly-Disassembly.Life (Basel, Switzerland) · 2021Article
- Modeling the complete kinetics of coxsackievirus B3 reveals human determinants of host-cell feedback.Cell systems · 2021Article
- In vitro assembly and evaluation of Nora virus VLPs.Acta virologica · 2021Article
- Viral structural proteins as targets for antivirals.Current opinion in virology · 2020Review
- Assembly of infectious enteroviruses depends on multiple, conserved genomic RNA-coat protein contacts.PLoS pathogens · 2020Article
- Article
- Evolutionary and Structural Overview of Human Picornavirus Capsid Antibody Evasion.Frontiers in cellular and infection microbiology · 2019Review
- Article
- The 3.3 Å structure of a plant geminivirus using cryo-EM.Nature communications · 2018Article
- A virus-like particle-based tetravalent vaccine for hand, foot, and mouth disease elicits broad and balanced protective immunity.Emerging microbes & infections · 2018Article
- The Cellular Chaperone Heat Shock Protein 90 Is Required for Foot-and-Mouth Disease Virus Capsid Precursor Processing and Assembly of Capsid Pentamers.Journal of virology · 2018Article
- Single Particle Observation of SV40 VP1 Polyanion-Induced Assembly Shows That Substrate Size and Structure Modulate Capsid Geometry.ACS chemical biology · 2017Article
- Genomic RNA folding mediates assembly of human parechovirus.Nature communications · 2017Article
- Honey Bee Deformed Wing Virus Structures Reveal that Conformational Changes Accompany Genome Release.Journal of virology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The Picornaviridae are a large family of small, spherical RNA viruses that includes numerous pathogens. The picornavirus structural proteins VP0, VP1, and VP3 are believed to first form protomers, which then form 14S particles and subsequently assemble to form empty and RNA-filled particles. 14S particles have long been presumed to be pentamers. However, the structure of the 14S particles, their mechanism of assembly, and the role of empty particles during infection are all unknown. We established an in vitro assembly system for bovine enterovirus (BEV) by using purified baculovirus-expressed proteins. By Rayleigh scattering, we determined that 14S particles are 488 kDa, confirming they are pentamers. Image reconstructions based on negative-stain electron microscopy showed that 14S particles have 5-fold symmetry, and their structures correlate extremely well with the corresponding pentamer from crystal structures of mature BEV. Purified 14S particles readily assemble in response to increasing ionic strength or temperature to form 5.8-MDa 12-pentamer particles, indistinguishable from native empty particles. Surprisingly, empty particles were sufficiently stable that, under physiological conditions, dissociation is unlikely to be a biologically relevant reaction. This suggests that empty particles are not a storage form of 14S particles, at least for bovine enterovirus, but are either a dead-end product or direct precursor into which viral RNA is packaged by as-yet-unidentified machinery.
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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.