ArticleJournal of virology2017
Heat Shock Protein 90 Ensures Efficient Mumps Virus Replication by Assisting with Viral Polymerase Complex Formation.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 62 citations in OpenAlex.
- HSPA5 induces autophagy targeting VP2 through the PERK-eIF2α signaling pathway to inhibit SVA replication.Journal of virology · 2026Article
- Mumps Virus: Replication, Immune Response, and the Changing Landscape of Vaccine Effectiveness.Pathogens (Basel, Switzerland) · 2026Review
- Functional dissection of the C-terminal domain of rabies virus RNA polymerase L protein.Journal of virology · 2025Article
- Structural and molecular properties of mumps virus inclusion bodies.Science advances · 2024Article
- Host proteins interact with viral elements and affect the life cycle of highly pathogenic avian influenza A virus H7N9.Heliyon · 2024Article
- HSP90 is part of a protein complex with the L polymerase of Rift Valley fever phlebovirus and prevents its degradation by the proteasome during the viral genome replication/transcription stage.Frontiers in cellular and infection microbiology · 2024Article
- Disruption of Ebola NPJournal of molecular biology · 2023Article
- Role of heat shock protein 90 as an antiviral target for swine enteric coronaviruses.Virus research · 2023Article
- Article
- 9-Butyl-Harmol Exerts Antiviral Activity against Newcastle Disease Virus through Targeting GSK-3β and HSP90β.Journal of virology · 2023Article
- Review
- SNARE protein USE1 is involved in the glycosylation and the expression of mumps virus fusion protein and important for viral propagation.PLoS pathogens · 2022Article
- Hsp90 Regulates GCRV-II Proliferation by Interacting with VP35 as Its Receptor and Chaperone.Journal of virology · 2022Article
- Nucleolar Protein Treacle Is Important for the Efficient Growth of Mumps Virus.Journal of virology · 2022Article
- Liquid Phase Partitioning in Virus Replication: Observations and Opportunities.Annual review of virology · 2022Review
- Tumor Temperature: Friend or Foe of Virus-Based Cancer Immunotherapy.Biomedicines · 2022Review
- Hsp90 Activity Is Necessary for the Maturation of Rabies Virus Polymerase.International journal of molecular sciences · 2022Article
- p17-Modulated Hsp90/Cdc37 Complex Governs Oncolytic Avian Reovirus Replication by Chaperoning p17, Which Promotes Viral Protein Synthesis and Accumulation of Viral Proteins σC and σA in Viral Factories.Journal of virology · 2022Article
- Heat shock proteins and viral infection.Frontiers in immunology · 2022Review
- Unique Tropism and Entry Mechanism of Mumps Virus.Viruses · 2021Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Paramyxoviral RNAs are synthesized by a viral RNA-dependent RNA polymerase (RdRp) consisting of the large (L) protein and its cofactor phosphoprotein (P protein). The L protein is a multifunctional protein that catalyzes RNA synthesis, mRNA capping, and mRNA polyadenylation. Growing evidence shows that the stability of several paramyxovirus L proteins is regulated by heat shock protein 90 (Hsp90). In this study, we demonstrated that Hsp90 activity was important for mumps virus (MuV) replication. The Hsp90 activity was required for L-protein stability and activity because an Hsp90-specific inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), destabilized the MuV L protein and suppressed viral RNA synthesis. However, once the L protein formed a mature polymerase complex with the P protein, Hsp90 activity was no longer required for the stability and activity of the L protein. When the Hsp90 activity was inhibited, the MuV L protein was degraded through the CHIP (C terminus of Hsp70-interacting protein)-mediated proteasomal pathway. High concentrations of 17-AAG showed strong cytotoxicity to certain cell types, but combined use of an Hsp70 inhibitor, VER155008, potentiated degradation of the L protein, allowing a sufficient reduction of 17-AAG concentration to block MuV replication with minimum cytotoxicity. Regulation of the L protein by Hsp90 and Hsp70 chaperones was also demonstrated for another paramyxovirus, the measles virus. Collectively, our data show that the Hsp90/Hsp70 chaperone machinery assists in the maturation of the paramyxovirus L protein and thereby in the formation of a mature RdRp complex and efficient viral replication.
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