ArticlePLoS pathogens2020
Cryo-EM structures reveal two distinct conformational states in a picornavirus cell entry intermediate.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
24 citing papers in PubMed, 28 citations in OpenAlex.
- Open questions in enterovirus uncoating.Journal of virology · 2026Review
- Review
- Structural insight into the assembly and D antigenicity of polio type 1 stabilized virus-like particles.NPJ vaccines · 2026Article
- New rhinovirus uncoating intermediate reveals how sodium versus potassium ions influence RNA release.Scientific reports · 2025Article
- Cryo-EM structure of the Seneca Valley virus A-particle and related structural states.Journal of virology · 2025Article
- Norovirus replication, host interactions and vaccine advances.Nature reviews. Microbiology · 2025Review
- Foot-and-mouth disease virus antigenic landscape and reduced immunogenicity elucidated in atomic detail.Nature communications · 2024Article
- Vaccine Potency and Structure of Yeast-Produced Polio Type 2 Stabilized Virus-like Particles.Vaccines · 2024Article
- Mechanism of enterovirus VP0 maturation cleavage based on the structure of a stabilised assembly intermediate.PLoS pathogens · 2024Article
- Mechanism of enterovirus VP0 maturation cleavage based on the structure of a stabilised assembly intermediate.bioRxiv : the preprint server for biology · 2024Article
- Cell Culture Adaptive Amino Acid Substitutions in FMDV Structural Proteins: A Key Mechanism for Altered Receptor Tropism.Viruses · 2024Review
- Virus-Receptor Interactions and Receptor-Mediated Virus Entry into Host Cells.Sub-cellular biochemistry · 2024Review
- A tradeoff between enterovirus A71 particle stability and cell entry.Nature communications · 2023Article
- Identification of a Conserved, Linear Epitope on VP3 ofViruses · 2023Article
- A conserved glutathione binding site in poliovirus is a target for antivirals and vaccine stabilisation.Communications biology · 2022Article
- Review
- Flexible, disposable photocatalytic plastic films for the destruction of viruses.Journal of photochemistry and photobiology. B, Biology · 2022Article
- Thermal stabilization of enterovirus A 71 and production of antigenically stabilized empty capsids.The Journal of general virology · 2022Article
- Atomic Structures of Coxsackievirus B5 Provide Key Information on Viral Evolution and Survival.Journal of virology · 2022Article
- Immune response to a conserved enteroviral epitope of the major capsid VP1 protein is associated with lower risk of cardiovascular disease.EBioMedicine · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
The virions of enteroviruses such as poliovirus undergo a global conformational change after binding to the cellular receptor, characterized by a 4% expansion, and by the opening of holes at the two and quasi-three-fold symmetry axes of the capsid. The resultant particle is called a 135S particle or A-particle and is thought to be on the pathway to a productive infection. Previously published studies have concluded that the membrane-interactive peptides, namely VP4 and the N-terminus of VP1, are irreversibly externalized in the 135S particle. However, using established protocols to produce the 135S particle, and single particle cryo-electron microscopy methods, we have identified at least two unique states that we call the early and late 135S particle. Surprisingly, only in the "late" 135S particles have detectable levels of the VP1 N-terminus been trapped outside the capsid. Moreover, we observe a distinct density inside the capsid that can be accounted for by VP4 that remains associated with the genome. Taken together our results conclusively demonstrate that the 135S particle is not a unique conformation, but rather a family of conformations that could exist simultaneously.
Indexed as
Identifiers
What OpenQuestion holds
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.