Evidence map›Paper›PMID 31516086›Full record

ArticleEmerging microbes & infections2019

Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription.

Jingliang Chen, Zhangping He, Yaochang Yuan, Feng Huang, Baohong Luo, Jianhua Zhang, Ting Pan, Hui Zhang, Junsong Zhang

Open access · goldAbstract read
In one paragraph

Article in Emerging microbes & infections, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  5. Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  8. Review
  9. Review
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  12. The ORF8 protein of SARS-CoV-2 mediates immune evasion through down-regulating MHC-Ι.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Review
  14. Negri bodies and other virus membrane-less replication compartments.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  15. Article
  16. Article
  17. 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

9 authors at 4 institutions in 3 countries.

Jingliang ChenInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Guangdong Engineering Research Center for Antimicrobial Agent and Immunotechnology, Zhongshan School of Medicine, Sun Yat-Sen University , Guangzhou , People's Republic of China.
Zhangping HeInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Guangdong Engineering Research Center for Antimicrobial Agent and Immunotechnology, Zhongshan School of Medicine, Sun Yat-Sen University , Guangzhou , People's Republic of China.
Yaochang YuanInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Guangdong Engineering Research Center for Antimicrobial Agent and Immunotechnology, Zhongshan School of Medicine, Sun Yat-Sen University , Guangzhou , People's Republic of China.
Feng HuangInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Guangdong Engineering Research Center for Antimicrobial Agent and Immunotechnology, Zhongshan School of Medicine, Sun Yat-Sen University , Guangzhou , People's Republic of China.
Baohong LuoInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Guangdong Engineering Research Center for Antimicrobial Agent and Immunotechnology, Zhongshan School of Medicine, Sun Yat-Sen University , Guangzhou , People's Republic of China.
Jianhua ZhangCAS Key Laboratory for Pathogenic Microbiology, Institute of Microbiology, Chinese Academy of Sciences , Beijing , People's Republic of China.
Ting PanInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Guangdong Engineering Research Center for Antimicrobial Agent and Immunotechnology, Zhongshan School of Medicine, Sun Yat-Sen University , Guangzhou , People's Republic of China.
Hui ZhangInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Guangdong Engineering Research Center for Antimicrobial Agent and Immunotechnology, Zhongshan School of Medicine, Sun Yat-Sen University , Guangzhou , People's Republic of China.
Junsong ZhangInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Guangdong Engineering Research Center for Antimicrobial Agent and Immunotechnology, Zhongshan School of Medicine, Sun Yat-Sen University , Guangzhou , People's Republic of China.
Sun Yat-sen University · CNChinese Academy of Sciences · CNCzech Academy of Sciences, Institute of Microbiology · CZMinistry of Education · BN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The polymerase complex of Ebola virus (EBOV) is the functional unit for transcription and replication of viral genome. Nucleoprotein (NP) is a multifunctional protein with high RNA binding affinity and recruits other viral proteins to form functional polymerase complex. In our study, we investigated host proteins associated with EBOV polymerase complex using NP as bait in a transcription and replication competent minigenome system by mass spectrometry analysis and identified SET and MYND domain-containing protein 3 (SMYD3) as a novel host protein which was required for the replication of EBOV. SMYD3 specifically interacted with NP and was recruited to EBOV inclusion bodies through NP. The depletion of SMYD3 dramatically suppressed EBOV mRNA production. A mimic of non-phosphorylated VP30, which is a transcription activator, could partially rescue the viral mRNA production downregulated by the depletion of SMYD3. In addition, SMYD3 promoted NP-VP30 interaction in a dose-dependent manner. These results revealed that SMYD3 was a novel host factor recruited by NP to supporting EBOV mRNA transcription through increasing the binding of VP30 to NP. Thus, our study provided a new understanding of mechanism underlying the transcription of EBOV genome, and a novel anti-EBOV drug design strategy by targeting SMYD3.

Indexed as

Host-Pathogen InteractionsTranscription, GeneticEbolavirusHEK293 CellsHistone-Lysine N-MethyltransferaseHumansMass SpectrometryNucleocapsid ProteinsProtein BindingProtein Interaction MappingRNA, MessengerRNA, ViralHistone-Lysine N-Methyltransferasenucleocapsid protein, Ebola virusNucleocapsid ProteinsRNA, MessengerRNA, ViralSMYD3 protein, humanEbola virusmRNA transcriptionNPSMYD3VP30

Identifiers

PMID31516086
PMCPMC6758638
OpenAlexW2972515495

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.