Evidence map›Paper›PMID 35442060›Full record

ArticleJournal of virology2022

Atomic Structures of Coxsackievirus B5 Provide Key Information on Viral Evolution and Survival.

Peng Yang, Dawei Shi, Jianmeng Fu, Li Zhang, Ruihong Chen, Binyang Zheng, Xiangxi Wang, Sihong Xu, Ling Zhu, Kang Wang

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.6field-weighted citation impact, top 16% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Open questions in enterovirus uncoating.Journal of virology · 2026
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Peng Yang *Key Laboratory of Infection and Immunity, Institute of Biophysicsgrid.418856.6, Chinese Academy of Sciences, Beijing, China.
Dawei Shi *Institute for In Vitro Diagnostics Control, National Institutes for Food and Drug Controlgrid.410749.f, Beijing, China.
Jianmeng FuKey Laboratory of Infection and Immunity, Institute of Biophysicsgrid.418856.6, Chinese Academy of Sciences, Beijing, China.
Li ZhangNational Health Commission of the People's Republic of China, Key Laboratory of Enteric Pathogenic Microbiology (Jiangsu Provincial Center for Disease Control and Prevention), Nanjing, China.
Ruihong ChenKey Laboratory of Infection and Immunity, Institute of Biophysicsgrid.418856.6, Chinese Academy of Sciences, Beijing, China.
Binyang ZhengNational Health Commission of the People's Republic of China, Key Laboratory of Enteric Pathogenic Microbiology (Jiangsu Provincial Center for Disease Control and Prevention), Nanjing, China.
Xiangxi WangKey Laboratory of Infection and Immunity, Institute of Biophysicsgrid.418856.6, Chinese Academy of Sciences, Beijing, China.
Sihong XuInstitute for In Vitro Diagnostics Control, National Institutes for Food and Drug Controlgrid.410749.f, Beijing, China.
Ling ZhuKey Laboratory of Infection and Immunity, Institute of Biophysicsgrid.418856.6, Chinese Academy of Sciences, Beijing, China.
Kang WangKey Laboratory of Infection and Immunity, Institute of Biophysicsgrid.418856.6, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0002-7467-1953
Chinese Academy of Sciences · CNJiangsu Provincial Center for Disease Control and Prevention · CNNational Institutes for Food and Drug Control · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coxsackie virus B5 (CVB5), a main serotype in human Enterovirus B (EVB), can cause severe viral encephalitis and aseptic meningitis among infants and children. Currently, there is no approved vaccine or antiviral therapy available against CVB5 infection. Here, we determined the atomic structures of CVB5 in three forms: mature full (F) particle (2.73 Å), intermediate altered (A) particle (2.81 Å), and procapsid empty (E) particle (2.95 Å). Structural analysis of F particle of CVB5 unveiled similar structures of "canyon," "puff," and "knob" as those other EV-Bs. We observed structural rearrangements that are alike during the transition from F to A particle, indicative of similar antigenicity, cell entry, and uncoating mechanisms shared by all EV-Bs. Further comparison of structures and sequences among all structure-known EV-Bs revealed that while the residues targeted by neutralizing MAbs are diversified and drive the evolution of EV-Bs, the relative conserved residues recognized by uncoating receptors could serve as the basis for the development of antiviral vaccines and therapeutics.

Indexed as

Enterovirus B, HumanBiological EvolutionCapsidCoxsackievirus InfectionsHumansProtein Domainsantiviral strategycryo-EM structureCVB5uncoatingviral evolutionviral survival

Identifiers

PMID35442060
PMCPMC9093117
OpenAlexW4224274641

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.