Evidence map›Paper›PMID 26750153›Full record

ArticleScientific reports2016

Human Heat shock protein 40 (Hsp40/DnaJB1) promotes influenza A virus replication by assisting nuclear import of viral ribonucleoproteins.

Jyoti Batra, Shashank Tripathi, Amrita Kumar, Jacqueline M Katz, Nancy J Cox, Renu B Lal, Suryaprakash Sambhara, Sunil K Lal

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

47 citing papers in PubMed, 68 citations in OpenAlex.

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  8. Proteomic profiling of pseudorabies virus-infected PK-15 cells based on 4D label free analysis.Veterinary research forum : an international quarterly journal · 2025
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  20. Heat shock proteins and viral infection.Frontiers in immunology · 2022
    Review
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

8 authors at 4 institutions in 3 countries.

Jyoti BatraSchool of Science, Monash University, Subang Jaya, Selangor, 47500, Malaysia.
Shashank TripathiVirology Group, International Centre for Genetic Engineering &Biotechnology, New Delhi, 110067, India.
Amrita KumarInfluenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta GA, 30333, USA.
Jacqueline M KatzInfluenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta GA, 30333, USA.
Nancy J CoxInfluenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta GA, 30333, USA.
Renu B LalInfluenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta GA, 30333, USA.
Suryaprakash SambharaInfluenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta GA, 30333, USA.
Sunil K LalSchool of Science, Monash University, Subang Jaya, Selangor, 47500, Malaysia.
Centers for Disease Control and Prevention · USInternational Centre for Genetic Engineering and Biotechnology · INMonash University Malaysia · MYNational Center for Immunization and Respiratory Diseases · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A unique feature of influenza A virus (IAV) life cycle is replication of the viral genome in the host cell nucleus. The nuclear import of IAV genome is an indispensable step in establishing virus infection. IAV nucleoprotein (NP) is known to mediate the nuclear import of viral genome via its nuclear localization signals. Here, we demonstrate that cellular heat shock protein 40 (Hsp40/DnaJB1) facilitates the nuclear import of incoming IAV viral ribonucleoproteins (vRNPs) and is important for efficient IAV replication. Hsp40 was found to interact with NP component of IAV RNPs during early stages of infection. This interaction is mediated by the J domain of Hsp40 and N-terminal region of NP. Drug or RNAi mediated inhibition of Hsp40 resulted in reduced nuclear import of IAV RNPs, diminished viral polymerase function and attenuates overall viral replication. Hsp40 was also found to be required for efficient association between NP and importin alpha, which is crucial for IAV RNP nuclear translocation. These studies demonstrate an important role for cellular chaperone Hsp40/DnaJB1 in influenza A virus life cycle by assisting nuclear trafficking of viral ribonucleoproteins.

Indexed as

Virus ReplicationBenzhydryl CompoundsCell LineCell NucleusGene Knockdown TechniquesHost-Pathogen InteractionsHSP40 Heat-Shock ProteinsHumansInfluenza A virusInfluenza, HumanModels, BiologicalProtein BindingProtein Interaction Domains and MotifsProtein TransportPyrrolidinonesRibonucleoproteinsBenzhydryl CompoundsHSP40 Heat-Shock ProteinsKNK 437PyrrolidinonesRibonucleoproteinsRNA, Small InterferingViral Proteins

Identifiers

PMID26750153
PMCPMC4707480
OpenAlexW2239597296

What OpenQuestion holds

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LicenceCC BY
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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.