ArticleNature microbiology2018
The TRiC chaperonin controls reovirus replication through outer-capsid folding.
Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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.
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Who cites it
45 citing papers in PubMed, 66 citations in OpenAlex.
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- A dsRNA Viral Transcriptional Regulator Evades Innate Immunity by Hijacking Host CoTranscription Factor DHX9.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The oncolytic avian reovirus p17 protein triggers chaperone-mediated autophagy by modulating Hsp90 and the T-complex protein-1 ring complex chaperones and co-chaperones to activate the IKK/NF-κB signaling.Journal of virology · 2025Article
- Annexin A2 stabilizes the endoplasmic reticulum and actin cytoskeleton and influences the formation of reovirus factories.Journal of virology · 2025Article
- Ataxin-2-like promotes translation of nonpolyadenylated reovirus mRNA.Nature communications · 2025Article
- Interactomics of SARS-CoV-2 Macrodomain 1 Reveals Putative Clients of ADP-ribosyl Hydrolase Activity.bioRxiv : the preprint server for biology · 2025Article
- Spatiotemporal coordination of reovirus peripheral core replication to perinuclear whole virus assembly.PLoS pathogens · 2025Article
- Prefoldin complex promotes interferon-stimulated gene expression and is inhibited by rotavirus VP3.Nature communications · 2025Article
- Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025Review
- Lassa virus Z protein hijacks the autophagy machinery for efficient transportation by interrupting CCT2-mediated cytoskeleton network formation.Autophagy · 2024Article
- Enterovirus-A71 exploits RAB11 to recruit chaperones for virus morphogenesis.Journal of biomedical science · 2024Article
- The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication.mBio · 2024Article
- Protein Quality Control Systems and ER Stress as Key Players in SARS-CoV-2-Induced Neurodegeneration.Cells · 2024Review
- Chaperonin TRiC/CCT subunit CCT7 is involved in the replication of canine parvovirus in F81 cells.Frontiers in microbiology · 2024Article
- Quantitative analysis of acetylation in peste des petits ruminants virus-infected Vero cells.Virology journal · 2023Article
- Elucidating cellular interactome of chikungunya virus identifies host dependency factors.Virologica Sinica · 2023Article
- Chaperonin TRiC/CCT Participates in Mammarenavirus Multiplication in Human Cells via Interaction with the Viral Nucleoprotein.Journal of virology · 2023Article
- 14th International dsRNA Virus Symposium, Banff, Alberta, Canada, 10-14 October 2022.Virus research · 2023Article
- Mechanistic insights into protein folding by the eukaryotic chaperonin complex CCT.Biochemical Society transactions · 2022Review
- Reovirus Activated Cell Death Pathways.Cells · 2022Review
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Viruses are molecular machines sustained through a life cycle that requires replication within host cells. Throughout the infectious cycle, viral and cellular components interact to advance the multistep process required to produce progeny virions. Despite progress made in understanding the virus-host protein interactome, much remains to be discovered about the cellular factors that function during infection, especially those operating at terminal steps in replication. In an RNA interference screen, we identified the eukaryotic chaperonin T-complex protein-1 (TCP-1) ring complex (TRiC; also called CCT for chaperonin containing TCP-1) as a cellular factor required for late events in the replication of mammalian reovirus. We discovered that TRiC functions in reovirus replication through a mechanism that involves folding the viral σ3 major outer-capsid protein into a form capable of assembling onto virus particles. TRiC also complexes with homologous capsid proteins of closely related viruses. Our data define a critical function for TRiC in the viral assembly process and raise the possibility that this mechanism is conserved in related non-enveloped viruses. These results also provide insight into TRiC protein substrates and establish a rationale for the development of small-molecule inhibitors of TRiC as potential antiviral therapeutics.
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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.