Evidence map›Paper›PMID 30987343›Full record

ArticleViruses2019

Mechanism of Inhibition of Ebola Virus RNA-Dependent RNA Polymerase by Remdesivir.

Egor P Tchesnokov, Joy Y Feng, Danielle P Porter, Matthias Götte

Abstract read
In one paragraph

Article in Viruses, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 321 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
321citing papers in PubMed, 1 pooled it
–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

321 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Remdesivir for the treatment of COVID-19.The Cochrane database of systematic reviews · 2021
    Pooled it
  2. Trial
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  18. Conserved Filovirus Proteins as Targets of Broad-Spectrum Antivirals.bioRxiv : the preprint server for biology · 2025
    Article
  19. Article
  20. Article

261 more citing papers are in PubMed but not listed here.

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

4 authors.

Egor P TchesnokovDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB T6G 2E1, Canada. tchesnok@ualberta.ca.
Joy Y FengGilead Sciences, Inc., Foster City, CA 94404, USA. Joy.Feng@gilead.com.
Danielle P PorterGilead Sciences, Inc., Foster City, CA 94404, USA. Danielle.Porter@gilead.com.
Matthias GötteDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB T6G 2E1, Canada. gotte@ualberta.ca.

Funding

CIHR 159507
6 · The paper itself

Abstract

Remdesivir (GS-5734) is a 1'-cyano-substituted adenosine nucleotide analogue prodrug that shows broad-spectrum antiviral activity against several RNA viruses. This compound is currently under clinical development for the treatment of Ebola virus disease (EVD). While antiviral effects have been demonstrated in cell culture and in non-human primates, the mechanism of action of Ebola virus (EBOV) inhibition for remdesivir remains to be fully elucidated. The EBOV RNA-dependent RNA polymerase (RdRp) complex was recently expressed and purified, enabling biochemical studies with the relevant triphosphate (TP) form of remdesivir and its presumptive target. In this study, we confirmed that remdesivir-TP is able to compete for incorporation with adenosine triphosphate (ATP). Enzyme kinetics revealed that EBOV RdRp and respiratory syncytial virus (RSV) RdRp incorporate ATP and remdesivir-TP with similar efficiencies. The selectivity of ATP against remdesivir-TP is ~4 for EBOV RdRp and ~3 for RSV RdRp. In contrast, purified human mitochondrial RNA polymerase (h-mtRNAP) effectively discriminates against remdesivir-TP with a selectivity value of ~500-fold. For EBOV RdRp, the incorporated inhibitor at position i does not affect the ensuing nucleotide incorporation event at position i+1. For RSV RdRp, we measured a ~6-fold inhibition at position i+1 although RNA synthesis was not terminated. Chain termination was in both cases delayed and was seen predominantly at position i+5. This pattern is specific to remdesivir-TP and its 1'-cyano modification. Compounds with modifications at the 2'-position show different patterns of inhibition. While 2'-C-methyl-ATP is not incorporated, ara-ATP acts as a non-obligate chain terminator and prevents nucleotide incorporation at position i+1. Taken together, our biochemical data indicate that the major contribution to EBOV RNA synthesis inhibition by remdesivir can be ascribed to delayed chain termination. The long distance of five residues between the incorporated nucleotide analogue and its inhibitory effect warrant further investigation.

Indexed as

AdenosineAdenosine MonophosphateAdenosine TriphosphateAlanineAntiviral AgentsDNA-Directed RNA PolymerasesEbolavirusEnzyme InhibitorsHumansKineticsMolecular StructureProdrugsRespiratory Syncytial Virus, HumanRibonucleotidesRNA-Dependent RNA PolymeraseRNA, ViralAdenosineAdenosine MonophosphateAdenosine TriphosphateAlanineAntiviral AgentsDNA-Directed RNA PolymerasesEnzyme InhibitorsProdrugsremdesivirRibonucleotidesRNA-Dependent RNA PolymeraseRNA, ViralViral Proteinsdelayed chain terminationEbola virusGS-5734RdRpremdesivirrespiratory syncytial virusRNA polymerase

Identifiers

PMID30987343
PMCPMC6520719

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.