ArticleCell host & microbe2021
Cryo-EM structures reveal the molecular basis of receptor-initiated coxsackievirus uncoating.
Article in Cell host & microbe, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 31 citations in OpenAlex.
- Cross-Neutralizing and Broadly Neutralizing Human Antibodies Against Nonenveloped Viruses.European journal of immunology · 2026Review
- A dual-receptor checkpoint primes enterovirus D68 for respiratory cell entry.Nature communications · 2026Article
- Open questions in enterovirus uncoating.Journal of virology · 2026Review
- In Silico Saturation-Mutagenesis-Based Genomic Mutation Risk Assessment for Enterovirus B.Viruses · 2026Article
- Coxsackie B1 virus-like particle that lacks VP4 protein demonstrates improved vaccine scalability, stability and immunogenicity.Journal of biomedical science · 2026Article
- Article
- Neutralizing human monoclonal antibodies to poliovirus map to the receptor binding site.Nature communications · 2026Article
- SPNS1 is an essential cellular factor for EV-A71 by acting as a transporter of viral pocket factor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A dual monoclonal antibody-based sandwich ELISA for detection of potent vaccine immunogen against Coxsackievirus B1.Virologica Sinica · 2025Article
- Article
- Immunological and structural evaluation of the intranasally administrated CVB1 whole-virus and VLP vaccines.Scientific reports · 2025Article
- A single residue switch mediates the broad neutralization of Rotaviruses.Nature communications · 2025Article
- Broadly therapeutic antibody provides cross-serotype protection against enteroviruses via Fc effector functions and by mimicking SCARB2.Nature microbiology · 2024Article
- Comparison of structure and immunogenicity of CVB1-VLP and inactivated CVB1 vaccine candidates.Research square · 2024Article
- A human monoclonal antibody binds within the poliovirus receptor-binding site to neutralize all three serotypes.Nature communications · 2023Article
- In silico epitope prediction and evolutionary analysis reveals capsid mutation patterns for enterovirus B.PloS one · 2023Article
- Investigating the mechanism of Echovirus 30 cell invasion.Frontiers in microbiology · 2023Review
- High-resolution structural analysis of enterovirus-reactive polyclonal antibodies in complex with whole virions.PNAS nexus · 2022Article
- Cryo-electron microscopy and image classification reveal the existence and structure of the coxsackievirus A6 virion.Communications biology · 2022Article
- Atomic Structures of Coxsackievirus B5 Provide Key Information on Viral Evolution and Survival.Journal of virology · 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
29 authors at 3 institutions in 2 countries.
Funding
Abstract
Enterovirus uncoating receptors bind at the surface depression ("canyon") that encircles each capsid vertex causing the release of a host-derived lipid called "pocket factor" that is buried in a hydrophobic pocket formed by the major viral capsid protein, VP1. Coxsackievirus and adenovirus receptor (CAR) is a universal uncoating receptor of group B coxsackieviruses (CVB). Here, we present five high-resolution cryoEM structures of CVB representing different stages of virus infection. Structural comparisons show that the CAR penetrates deeper into the canyon than other uncoating receptors, leading to a cascade of events: collapse of the VP1 hydrophobic pocket, high-efficiency release of the pocket factor and viral uncoating and genome release under neutral pH, as compared with low pH. Furthermore, we identified a potent therapeutic antibody that can neutralize viral infection by interfering with virion-CAR interactions, destabilizing the capsid and inducing virion disruption. Together, these results define the structural basis of CVB cell entry and antibody neutralization.
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.