ArticleJournal of virology2004
Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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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.
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Who cites it
52 citing papers in PubMed, 78 citations in OpenAlex.
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- A chicken interferon stimulated gene screen reveals limited genes restricting influenza replication.bioRxiv : the preprint server for biology · 2026Article
- Oncolytic Vaccinia Virus-HSP70-shRNA Amplifies Viral Replication, ROS/Autophagy, and Immunity to Fight Colorectal Cancer.Cancer science · 2026Article
- Heat shock protein 70 enhances viral replication by stabilizing Senecavirus A nonstructural proteins L and 3D.Veterinary research · 2024Article
- Influenza B viruses are more susceptible to high temperatures than influenza A viruses.Npj viruses · 2024Article
- Photothermal treatment-based heat stress regulates function of myeloid-derived suppressor cells.Scientific reports · 2024Article
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- Host cell stress response as a predictor of COVID-19 infectivity and disease progression.Frontiers in molecular biosciences · 2022Review
- Gene Expression Signatures Reveal Common Virus Infection Pathways in Target Tissues of Type 1 Diabetes, Hashimoto's Thyroiditis, and Celiac Disease.Frontiers in immunology · 2022Article
- Elevated temperature inhibits SARS-CoV-2 replication in respiratory epithelium independently of IFN-mediated innate immune defenses.PLoS biology · 2021Article
- Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection.International journal of molecular sciences · 2021Review
- Effect of a fever in viral infections - the 'Goldilocks' phenomenon?World journal of clinical cases · 2021Review
- Possible Therapeutic Intervention Strategies for COVID-19 by Manipulating the Cellular Proteostasis Network.Advances in experimental medicine and biology · 2021Article
- Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development.Signal transduction and targeted therapy · 2020Review
- SARS-CoV-2: At the Crossroad Between Aging and Neurodegeneration.Movement disorders : official journal of the Movement Disorder Society · 2020Article
- Avian Chaperonin Containing TCP1 Subunit 5 Supports Influenza A Virus Replication by Interacting With Viral Nucleoprotein, PB1, and PB2 Proteins.Frontiers in microbiology · 2020Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The influenza virus genome replicates and forms a viral ribonucleoprotein complex (vRNP) with nucleoprotein (NP) and RNA polymerases in the nuclei of host cells. vRNP is then exported into the cytoplasm for viral morphogenesis at the cell membrane. Matrix protein 1 (M1) and nonstructural protein 2/nuclear export protein (NS2/NEP) work in the nuclear export of vRNP by associating with it. It was previously reported that influenza virus production was inhibited in Madin-Darby canine kidney (MDCK) cells cultured at 41 degrees C because nuclear export of vRNP was blocked by the dissociation of M1 from vRNP (A. Sakaguchi, E. Hirayama, A. Hiraki, Y. Ishida, and J. Kim, Virology 306:244-253, 2003). Previous data also suggested that a certain protein(s) synthesized only at 41 degrees C inhibited the association of M1 with vRNP. The potential of heat shock protein 70 (HSP70) as a candidate obstructive protein was investigated. Induction of HSP70 by prostaglandin A1 (PGA1) at 37 degrees C caused the suppression of virus production. The nuclear export of viral proteins was inhibited by PGA1, and M1 was not associated with vRNP, indicating that HSP70 prevents M1 from binding to vRNP. An immunoprecipitation assay showed that HSP70 was bound to vRNP, suggesting that the interaction of HSP70 with vRNP is the reason for the dissociation of M1. Moreover, NS2 accumulated in the nucleoli of host cells cultured at 41 degrees C, showing that the export of NS2 was also disturbed at 41 degrees C. However, NS2 was exported normally from the nucleus, irrespective of PGA1 treatment at 37 degrees C, suggesting that HSP70 does not influence NS2.
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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.