Evidence map›Paper›PMID 30814282›Full record

ArticleJournal of virology2019

Hsp27 Responds to and Facilitates Enterovirus A71 Replication by Enhancing Viral Internal Ribosome Entry Site-Mediated Translation.

Xuelian Dan, Qianya Wan, Lina Yi, Jing Lu, Yang Jiao, Huangcan Li, Dan Song, Ying Chen, Hongxi Xu, Ming-Liang He

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
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  13. Heat shock proteins and viral infection.Frontiers in immunology · 2022
    Review
  14. Review
  15. Article
  16. Review
  17. Translation control of Enterovirus A71 gene expression.Journal of biomedical science · 2020
    Review
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Xuelian DanDepartment of Biomedical Sciences, City University of Hong Kong, Kowloon, Hong Kong.
Qianya WanDepartment of Biomedical Sciences, City University of Hong Kong, Kowloon, Hong Kong.
Lina YiGuangdong Provincial Institution of Public Health, Guangdong Center for Disease Control and Prevention, Guangzhou, China.ORCID 0000-0003-1122-6999
Jing LuGuangdong Provincial Institution of Public Health, Guangdong Center for Disease Control and Prevention, Guangzhou, China.
Yang JiaoDepartment of Biomedical Sciences, City University of Hong Kong, Kowloon, Hong Kong.
Huangcan LiDepartment of Biomedical Sciences, City University of Hong Kong, Kowloon, Hong Kong.
Dan SongDepartment of Biomedical Sciences, City University of Hong Kong, Kowloon, Hong Kong.
Ying ChenDepartment of Biomedical Sciences, City University of Hong Kong, Kowloon, Hong Kong.
Hongxi XuSchool of Pharmacy, Shanghai University of Traditional Chinese Medicine, Shanghai, People's Republic of China.
Ming-Liang HeDepartment of Biomedical Sciences, City University of Hong Kong, Kowloon, Hong Kong mlhe7788@gmail.com.
City University of Hong Kong · HKGuangdong Provincial Center for Disease Control and Prevention · CNShanghai University of Traditional Chinese Medicine · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enterovirus 71 (EV-A71) is a human pathogen that causes hand, foot, and mouth disease (HFMD) and fatal neurological diseases, and no effective treatment is available. Characterization of key host factors is important for understanding its pathogenesis and developing antiviral drugs. Here we report that Hsp27 is one of the most upregulated proteins in response to EV-A71 infection, as revealed by two-dimensional gel electrophoresis-based proteomics studies. Depletion of Hsp27 by small interfering RNA or CRISPR/Cas9-mediated knockout significantly inhibited viral replication, protein expression, and reproduction, while restoration of Hsp27 restored such virus activities. Furthermore, we show that Hsp27 plays a crucial role in regulating viral internal ribosome entry site (IRES) activities by two different mechanisms. Hsp27 markedly promoted 2A

Indexed as

Gene Expression Regulation, ViralInternal Ribosome Entry SitesProtein BiosynthesisCell Line, TumorCell NucleusCytoplasmEnterovirus A, HumanEnterovirus InfectionsEukaryotic Initiation Factor-4GFructose-BisphosphataseGene Knockout TechniquesHeat-Shock ProteinsHeterogeneous Nuclear Ribonucleoprotein A1HumansMolecular ChaperonesViral ProteinsEIF4G1 protein, humanEukaryotic Initiation Factor-4GFBP1 protein, humanFructose-BisphosphataseHeat-Shock ProteinsHeterogeneous Nuclear Ribonucleoprotein A1HSPB1 protein, humanInternal Ribosome Entry SitesMolecular ChaperonesViral ProteinsCRISPR/Cas9enterovirus A71heat shock protein 27hnRNP A1IRES

Identifiers

PMID30814282
PMCPMC6475798
OpenAlexW2916387662

What OpenQuestion holds

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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.