Evidence map›Paper›PMID 35107368›Full record

ArticleJournal of virology2022

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.

Wei-Ru Huang, Jyun-Yi Li, Yi-Ying Wu, Tsai-Ling Liao, Brent L Nielsen, Hung-Jen Liu

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Oncolytic avian reovirus-sensitized tumor infiltrating CD8Cell communication and signaling : CCS · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Wei-Ru HuangInstitute of Molecular Biology, National Chung Hsing Universitygrid.260542.7, Taichung, Taiwan.
Jyun-Yi LiInstitute of Molecular Biology, National Chung Hsing Universitygrid.260542.7, Taichung, Taiwan.
Yi-Ying WuInstitute of Molecular Biology, National Chung Hsing Universitygrid.260542.7, Taichung, Taiwan.
Tsai-Ling LiaoDepartment of Medical Research, Taichung Veterans General Hospital, Taichung, Taiwan.
Brent L NielsenDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, Utah, USA.
Hung-Jen LiuInstitute of Molecular Biology, National Chung Hsing Universitygrid.260542.7, Taichung, Taiwan.ORCID 0000-0002-1460-1494
National Chung Hsing University · TWBrigham Young University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this work we have determined that heat shock protein 90 (Hsp90) is essential for avian reovirus (ARV) replication by chaperoning the ARV p17 protein. p17 modulates the formation of the Hsp90/Cdc37 complex by phosphorylation of Cdc37, and this chaperone machinery protects p17 from ubiquitin-proteasome degradation. Inhibition of the Hsp90/Cdc37 complex by inhibitors (17-N-allylamino-17-demethoxygeldanamycin 17-AGG, and celastrol) or short hairpin RNAs (shRNAs) significantly reduced expression levels of viral proteins and virus yield, suggesting that the Hsp90/Cdc37 chaperone complex functions in virus replication. The expression levels of p17 were decreased at the examined time points (2 to 7 h and 7 to 16 h) in 17-AAG-treated cells in a dose-dependent manner while the expression levels of viral proteins σA, σC, and σNS were decreased at the examined time point (7 to 16 h). Interestingly, the expression levels of σC, σA, and σNS proteins increased along with coexpression of p17 protein. p17 together with the Hsp90/Cdc37 complex does not increase viral genome replication but enhances viral protein stability, maturation, and virus production. Virus factories of ARV are composed of nonstructural proteins σNS and μNS. We found that the Hsp90/Cdc37 chaperone complex plays an important role in accumulation of the outer-capsid protein σC, inner core protein σA, and nonstructural protein σNS of ARV in viral factories. Depletion of Hsp90 inhibited σA, σC, and p17 proteins colocalized with σNS in viral factories. This study provides novel insights into p17-modulated formation of the Hsp90/Cdc37 chaperone complex governing virus replication via stabilization and maturation of viral proteins and accumulation of viral proteins in viral factories for virus assembly.

Indexed as

Cell Cycle ProteinsChaperoninsHSP90 Heat-Shock ProteinsOrthoreovirus, AvianViral ProteinsVirus ReplicationAnimalsCapsid ProteinsGenome, ViralProteasome Endopeptidase ComplexUbiquitinViral Envelope Proteinsassembly factor P17Capsid ProteinsCDC37 protein, humanCell Cycle ProteinsChaperoninsHSP90 Heat-Shock ProteinsProteasome Endopeptidase ComplexUbiquitinViral Envelope ProteinsViral Proteinsavian reovirusHsp90/Cdc37 chaperone machineryinner core protein σAnonstructural protein p17nonstructural protein σNSouter-capsid protein σCviral factory

Identifiers

PMID35107368
PMCPMC8941905
OpenAlexW4210778818

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.