ArticleJournal of virology2014
Kinetic and structural analysis of coxsackievirus B3 receptor interactions and formation of the A-particle.
Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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
37 citing papers in PubMed, 47 citations in OpenAlex.
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- Discovery of a broad-spectrum monoclonal antibody recognizing a conserved, linear epitope WFYDGYPT on VP1 protein of Enterovirus A species.Virology journal · 2024Article
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- Baicalein suppresses Coxsackievirus B3 replication by inhibiting caspase-1 and viral protease 2A.Virologica Sinica · 2024Article
- In silico epitope prediction and evolutionary analysis reveals capsid mutation patterns for enterovirus B.PloS one · 2023Article
- Tradeoffs for a viral mutant with enhanced replication speed.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Broadly neutralizing monoclonal antibodies protect against multiple tick-borne flaviviruses.The Journal of experimental medicine · 2021Article
- Coxsackievirus B3-Its Potential as an Oncolytic Virus.Viruses · 2021Review
- Cryo-EM structures reveal the molecular basis of receptor-initiated coxsackievirus uncoating.Cell host & microbe · 2021Article
- Antivirals blocking entry of enteroviruses and therapeutic potential.Journal of biomedical science · 2021Review
- Single-Point Mutations within the Coxsackie B Virus Receptor-Binding Site Promote Resistance against Soluble Virus Receptor Traps.Journal of virology · 2020Article
- Cryo-EM structures reveal two distinct conformational states in a picornavirus cell entry intermediate.PLoS pathogens · 2020Article
- Albumin Enhances the Rate at Which Coxsackievirus B3 Strain 28 Converts to A-Particles.Journal of virology · 2020Article
- Extracellular Albumin and Endosomal Ions Prime Enterovirus Particles for Uncoating That Can Be Prevented by Fatty Acid Saturation.Journal of virology · 2019Article
- Article
- Unexpected mode of engagement between enterovirus 71 and its receptor SCARB2.Nature microbiology · 2019Article
- Atomic structures of enterovirus D68 in complex with two monoclonal antibodies define distinct mechanisms of viral neutralization.Nature microbiology · 2019Article
- Evolutionary and Structural Overview of Human Picornavirus Capsid Antibody Evasion.Frontiers in cellular and infection microbiology · 2019Review
- High-Resolution Structure Analysis of Antibody V5 and U4 Conformational Epitopes on Human Papillomavirus 16.Viruses · 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
5 authors at 3 institutions in 1 country.
Funding
Abstract
unlabelledThe coxsackievirus and adenovirus receptor (CAR) has been identified as the cellular receptor for group B coxsackieviruses, including serotype 3 (CVB3). CAR mediates infection by binding to CVB3 and catalyzing conformational changes in the virus that result in formation of the altered, noninfectious A-particle. Kinetic analyses show that the apparent first-order rate constant for the inactivation of CVB3 by soluble CAR (sCAR) at physiological temperatures varies nonlinearly with sCAR concentration. Cryo-electron microscopy (cryo-EM) reconstruction of the CVB3-CAR complex resulted in a 9.0-Å resolution map that was interpreted with the four available crystal structures of CAR, providing a consensus footprint for the receptor binding site. The analysis of the cryo-EM structure identifies important virus-receptor interactions that are conserved across picornavirus species. These conserved interactions map to variable antigenic sites or structurally conserved regions, suggesting a combination of evolutionary mechanisms for receptor site preservation. The CAR-catalyzed A-particle structure was solved to a 6.6-Å resolution and shows significant rearrangement of internal features and symmetric interactions with the RNA genome. IMPORTANCE: This report presents new information about receptor use by picornaviruses and highlights the importance of attaining at least an ∼9-Å resolution for the interpretation of cryo-EM complex maps. The analysis of receptor binding elucidates two complementary mechanisms for preservation of the low-affinity (initial) interaction of the receptor and defines the kinetics of receptor-catalyzed conformational change to the A-particle.
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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.