ArticleJournal of virology2005
The cellular chaperone heat shock protein 90 facilitates Flock House virus RNA replication in Drosophila cells.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
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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.
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.
Who cites it
49 citing papers in PubMed, 88 citations in OpenAlex.
- Influence of Hyperthermia Treatment on Varroa Infestation, Viral Infections, and Honey Bee Health in Beehives.Insects · 2025Review
- 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
- Review
- Multiple isoforms of HSP70 and HSP90 required for betanodavirus multiplication in medaka cells.Archives of virology · 2022Article
- Chemical Stimulants and Stressors Impact the Outcome of Virus Infection and Immune Gene Expression in Honey Bees (Frontiers in immunology · 2021Article
- Article
- Targeting host lipid flows: Exploring new antiviral and antibiotic strategies.Cellular microbiology · 2019Review
- Antiviral and Anti-Inflammatory Activities of Pochonin D, a Heat Shock Protein 90 Inhibitor, against Rhinovirus Infection.Biomolecules & therapeutics · 2018Article
- Defense Mechanisms against Viral Infection inViruses · 2018Review
- Virus and dsRNA-triggered transcriptional responses reveal key components of honey bee antiviral defense.Scientific reports · 2017Article
- A furoviral replicase recruits host HSP70 to membranes for viral RNA replication.Scientific reports · 2017Article
- The RNA binding of protein A from Wuhan nodavirus is mediated by mitochondrial membrane lipids.Virology · 2014Article
- The hop-like stress-induced protein 1 cochaperone is a novel cell-intrinsic restriction factor for mitochondrial tombusvirus replication.Journal of virology · 2014Article
- Article
- Flock house virus RNA polymerase initiates RNA synthesis de novo and possesses a terminal nucleotidyl transferase activity.PloS one · 2014Article
- Viruses and antiviral immunity in Drosophila.Developmental and comparative immunology · 2014Review
- Characterization of a nodavirus replicase revealed a de novo initiation mechanism of RNA synthesis and terminal nucleotidyltransferase activity.The Journal of biological chemistry · 2013Article
- The role of mutational robustness in RNA virus evolution.Nature reviews. Microbiology · 2013Review
- The C8ORF38 homologue Sicily is a cytosolic chaperone for a mitochondrial complex I subunit.The Journal of cell biology · 2013Article
- Broad action of Hsp90 as a host chaperone required for viral replication.Biochimica et biophysica acta · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The assembly of viral RNA replication complexes on intracellular membranes represents a critical step in the life cycle of positive-strand RNA viruses. We investigated the role of the cellular chaperone heat shock protein 90 (Hsp90) in viral RNA replication complex assembly and function using Flock House virus (FHV), an alphanodavirus whose RNA-dependent RNA polymerase, protein A, is essential for viral RNA replication complex assembly on mitochondrial outer membranes. The Hsp90 chaperone complex transports cellular mitochondrial proteins to the outer mitochondrial membrane import receptors, and thus we hypothesized that Hsp90 may also facilitate FHV RNA replication complex assembly or function. Treatment of FHV-infected Drosophila S2 cells with the Hsp90-specific inhibitor geldanamycin or radicicol potently suppressed the production of infectious virions and the accumulation of protein A and genomic, subgenomic, and template viral RNA. In contrast, geldanamycin did not inhibit the activity of preformed FHV RNA replication complexes. Hsp90 inhibitors also suppressed viral RNA and protein A accumulation in S2 cells expressing an FHV RNA replicon. Furthermore, Hsp90 inhibition with either geldanamycin or RNAi-mediated chaperone downregulation suppressed protein A accumulation in the absence of viral RNA replication. These results identify Hsp90 as a host factor involved in FHV RNA replication and suggest that FHV uses established cellular chaperone pathways to assemble its RNA replication complexes on intracellular membranes.
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Registered trials
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.