Evidence map›Paper›PMID 24474693›Full record

ArticleThe Journal of biological chemistry2014

Heat shock protein 70 modulates influenza A virus polymerase activity.

Rashid Manzoor, Kazumichi Kuroda, Reiko Yoshida, Yoshimi Tsuda, Daisuke Fujikura, Hiroko Miyamoto, Masahiro Kajihara, Hiroshi Kida, Ayato Takada

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.

  1. Pooled it
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  16. Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection.International journal of molecular sciences · 2021
    Review
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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

9 authors at 3 institutions in 2 countries.

Rashid ManzoorFrom the Division of Global Epidemiology, Research Center for Zoonosis Control and.
Kazumichi Kuroda
Reiko Yoshida
Yoshimi Tsuda
Daisuke Fujikura
Hiroko Miyamoto
Masahiro Kajihara
Hiroshi Kida
Ayato Takada
Hokkaido University · JPNihon University · JPUniversity of Zambia · ZM

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of heat shock protein 70 (Hsp70) in virus replication has been discussed for many viruses. The known suppressive role of Hsp70 in influenza virus replication is based on studies conducted in cells with various Hsp70 expression levels. In this study, we determined the role of Hsp70 in influenza virus replication in HeLa and HEK293T cells, which express Hsp70 constitutively. Co-immunoprecipitation and immunofluorescence studies revealed that Hsp70 interacted with PB2 or PB1 monomers and PB2/PB1 heterodimer but not with the PB1/PA heterodimer or PB2/PB1/PA heterotrimer and translocated into the nucleus with PB2 monomers or PB2/PB1 heterodimers. Knocking down Hsp70 resulted in reduced virus transcription and replication activities. Reporter gene assay, immunofluorescence assay, and Western blot analysis of nuclear and cytoplasmic fractions from infected cells demonstrated that the increase in viral polymerase activity during the heat shock phase was accompanied with an increase in Hsp70 and viral polymerases levels in the nuclei, where influenza virus replication takes place, whereas a reduction in viral polymerase activity was accompanied with an increase in cytoplasmic relocation of Hsp70 along with viral polymerases. Moreover, significantly higher levels of viral genomic RNA (vRNA) were observed during the heat shock phase than during the recovery phase. Overall, for the first time, these findings suggest that Hsp70 may act as a chaperone for influenza virus polymerase, and the modulatory effect of Hsp70 appears to be a sequel of shuttling of Hsp70 between nuclear and cytoplasmic compartments.

Indexed as

Virus ReplicationCell NucleusCytoplasmGene Expression Regulation, ViralHEK293 CellsHeLa CellsHSP70 Heat-Shock ProteinsHumansInfluenza A virusMicroscopy, FluorescenceNF-kappa BPlasmidsRNA, ViralSubcellular FractionsTranscription, GeneticViral ProteinsHSP70 Heat-Shock ProteinsNF-kappa BPB2 protein, influenza virusRNA, ViralViral ProteinsCell FractionationHeat ShockHeat Shock Protein 70Influenza VirusNF-kappa B (NF-kB)RNA VirusesViral PolymeraseViral Replication

Identifiers

PMID24474693
PMCPMC3953273
OpenAlexW2007732647

What OpenQuestion holds

Textmetadata
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.