Evidence map›Paper›PMID 33179566›Full record

ArticleEmerging microbes & infections2020

Human coronavirus dependency on host heat shock protein 90 reveals an antiviral target.

Cun Li, Hin Chu, Xiaojuan Liu, Man Chun Chiu, Xiaoyu Zhao, Dong Wang, Yuxuan Wei, Yuxin Hou, Huiping Shuai, Jianpiao Cai and 3 more

Abstract read
In one paragraph

Article in Emerging microbes & infections, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact
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

40 citing papers in PubMed.

  1. Article
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  7. Review
  8. Article
  9. Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  10. Article
  11. Review
  12. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Cun LiState Key Laboratory of Emerging Infectious Diseases, The University of Hong Kong, Hong Kong, People's Republic of China.
Hin ChuState Key Laboratory of Emerging Infectious Diseases, The University of Hong Kong, Hong Kong, People's Republic of China.
Xiaojuan LiuDepartment of Microbiology, The University of Hong Kong, Hong Kong, People's Republic of China.
Man Chun ChiuDepartment of Microbiology, The University of Hong Kong, Hong Kong, People's Republic of China.ORCID https://orcid.org/0000-0001-9503-6396
Xiaoyu ZhaoDepartment of Microbiology, The University of Hong Kong, Hong Kong, People's Republic of China.
Dong WangDepartment of Microbiology, The University of Hong Kong, Hong Kong, People's Republic of China.
Yuxuan WeiDepartment of Microbiology, The University of Hong Kong, Hong Kong, People's Republic of China.
Yuxin HouDepartment of Microbiology, The University of Hong Kong, Hong Kong, People's Republic of China.
Huiping ShuaiDepartment of Microbiology, The University of Hong Kong, Hong Kong, People's Republic of China.
Jianpiao CaiDepartment of Microbiology, The University of Hong Kong, Hong Kong, People's Republic of China.
Jasper Fuk-Woo ChanState Key Laboratory of Emerging Infectious Diseases, The University of Hong Kong, Hong Kong, People's Republic of China.ORCID https://orcid.org/0000-0001-6336-6657
Jie ZhouState Key Laboratory of Emerging Infectious Diseases, The University of Hong Kong, Hong Kong, People's Republic of China.
Kwok Yung YuenState Key Laboratory of Emerging Infectious Diseases, The University of Hong Kong, Hong Kong, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rapid accumulation of viral proteins in host cells render viruses highly dependent on cellular chaperones including heat shock protein 90 (Hsp90). Three highly pathogenic human coronaviruses, including MERS-CoV, SARS-CoV and SARS-CoV-2, have emerged in the past 2 decades. However, there is no approved antiviral agent against these coronaviruses. We inspected the role of Hsp90 for coronavirus propagation. First, an Hsp90 inhibitor, 17-AAG, significantly suppressed MERS-CoV propagation in cell lines and physiological-relevant human intestinal organoids. Second, siRNA depletion of Hsp90β, but not Hsp90α, significantly restricted MERS-CoV replication and abolished virus spread. Third, Hsp90β interaction with MERS-CoV nucleoprotein (NP) was revealed in a co-immunoprecipitation assay. Hsp90β is required to maintain NP stability. Fourth, 17-AAG substantially inhibited the propagation of SARS-CoV and SARS-CoV-2. Collectively, Hsp90 is a host dependency factor for human coronavirus MERS-CoV, SARS-CoV and SARS-COV-2. Hsp90 inhibitors can be repurposed as a potent and broad-spectrum antiviral against human coronaviruses.

Indexed as

A549 CellsAnimalsAntiviral AgentsBenzoquinonesCell LineChlorocebus aethiopsCOVID-19 Drug TreatmentHEK293 CellsHost Microbial InteractionsHSP90 Heat-Shock ProteinsHumansIntestinesLactams, MacrocyclicMiddle East Respiratory Syndrome CoronavirusOrgan Culture TechniquesRNA, Small InterferingAntiviral AgentsBenzoquinonesHSP90 Heat-Shock ProteinsLactams, MacrocyclicRNA, Small InterferingtanespimycinCoronavirusHsp90βnucleoproteinSARS-CoV-2viral replication

Identifiers

PMID33179566
PMCPMC7751432

What OpenQuestion holds

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LicenceCC BY
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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.