Evidence map›Paper›PMID 24530452›Full record

ArticleAntiviral research2014

Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase.

Ying Sun, Zidao Wang, Jiali Tao, Yi Wang, Andong Wu, Ziwen Yang, Kaimei Wang, Liqiao Shi, Yu Chen, Deyin Guo

Abstract read
In one paragraph

Article in Antiviral research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Inhibitors of DNA Methylation.Advances in experimental medicine and biology · 2022
    Review
  7. Review
  8. Structure-function analysis of the nsp14 N7-guanine methyltransferase reveals an essential role inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Enzymatic Assays to Explore Viral mRNA Capping Machinery.Chembiochem : a European journal of chemical biology · 2021
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article
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

10 authors.

Ying SunState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Zidao WangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Jiali TaoState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Yi WangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Andong WuState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Ziwen YangBiological Pesticide Engineering Research Center, Hubei Academy of Agricultural Science, Hubei 430072, PR China.
Kaimei WangBiological Pesticide Engineering Research Center, Hubei Academy of Agricultural Science, Hubei 430072, PR China.
Liqiao ShiBiological Pesticide Engineering Research Center, Hubei Academy of Agricultural Science, Hubei 430072, PR China.
Yu ChenState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China. Electronic address: chenyu@whu.edu.cn.
Deyin GuoState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China. Electronic address: dguo@whu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 5'-cap structure is a distinct feature of eukaryotic mRNAs and is important for RNA stability and protein translation by providing a molecular signature for the distinction of self or non-self mRNA. Eukaryotic viruses generally modify the 5'-end of their RNAs to mimic the cellular mRNA structure, thereby facilitating viral replication in host cells. However, the molecular organization and biochemical mechanisms of the viral capping apparatus typically differ from its cellular counterpart, which makes viral capping enzymes attractive targets for drug discovery. Our previous work showed that SARS coronavirus (SARS-CoV) non-structural protein 14 represents a structurally novel and unique guanine-N7-methyltransferase (N7-MTase) that is able to functionally complement yeast cellular N7-MTase. In the present study, we developed a yeast-based system for identifying and screening inhibitors against coronavirus N7-MTase using both 96-well and 384-well microtiter plates. The MTase inhibitors previously identified by in vitro biochemical assays were tested, and some, such as sinefungin, effectively suppressed N7-MTase in the yeast system. However, other compounds, such as ATA and AdoHcy, did not exert an inhibitory effect within a cellular context. These results validated the yeast assay system for inhibitor screening yet also demonstrated the difference between cell-based and in vitro biochemical assays. The yeast system was applied to the screening of 3000 natural product extracts, and three were observed to more potently inhibit the activity of coronavirus than human N7-MTase.

Indexed as

High-Throughput Screening AssaysAntiviral AgentsBiological ProductsCoronavirusDose-Response Relationship, DrugEnzyme ActivationEnzyme InhibitorsGuanineInhibitory Concentration 50MethyltransferasesRNA CapsSevere acute respiratory syndrome-related coronavirusYeastsAntiviral AgentsBiological ProductsEnzyme InhibitorsGuanineMethyltransferasesRNA CapsCoronavirusInhibitorN7-methyltransferasensp14SinefunginYeast

Identifiers

PMID24530452
PMCPMC7119097

What OpenQuestion holds

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Registered trials

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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.