Evidence map›Paper›PMID 26149721›Full record

ArticleVirology2015

A G-quadruplex-binding macrodomain within the "SARS-unique domain" is essential for the activity of the SARS-coronavirus replication-transcription complex.

Yuri Kusov, Jinzhi Tan, Enrique Alvarez, Luis Enjuanes, Rolf Hilgenfeld

Abstract read
In one paragraph

Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
7.8field-weighted citation impact, top 4% 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

80 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
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  7. Torsional twist of the SARS-CoV and SARS-CoV-2 SUD-N and SUD-M domains.Protein science : a publication of the Protein Society · 2025
    Article
  8. Article
  9. Torsional Twist of the SARS-CoV and SARS-CoV-2 SUD-N and SUD-M domains.bioRxiv : the preprint server for biology · 2024
    Article
  10. Article
  11. Review
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  14. SARS-CoV-2 Mac1 is required for IFN antagonism and efficient virus replication in cell culture and in mice.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Nsp3-N interactions are critical for SARS-CoV-2 fitness and virulence.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Review
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20 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

5 authors at 3 institutions in 2 countries.

Yuri KusovInstitute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Lübeck, Germany; German Center for Infection Research (DZIF), Hamburg - Lübeck - Borstel Site, University of Lübeck, Germany. Electronic address: koussov@biochem.uni-luebeck.de.
Jinzhi TanInstitute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Lübeck, Germany. Electronic address: tanjinzhi@gmail.com.
Enrique AlvarezDepartment of Molecular and Cell Biology, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma, Madrid, Spain. Electronic address: ealvarezmba@gmail.com.
Luis EnjuanesDepartment of Molecular and Cell Biology, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma, Madrid, Spain. Electronic address: L.enjuanes@cnb.csic.es.
Rolf HilgenfeldInstitute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Lübeck, Germany; German Center for Infection Research (DZIF), Hamburg - Lübeck - Borstel Site, University of Lübeck, Germany. Electronic address: hilgenfeld@biochem.uni-luebeck.de.
Centro Nacional de Biotecnología · ESGerman Center for Infection Research · DEUniversity of Lübeck · DE

Funding

SARS-CoV Proteins in Heterologous Viral InfectionP01AI060699 · NIAID · UNIVERSITY OF IOWA · PI PERLMAN, STANLEY · 2004 to 2021
$21.5M
NIAID NIH HHS 2P01AI060699-06A1NIAID NIH HHS HHSN266200700010CNIAID NIH HHS P01 AI060699PHS HHS CRIP-HHSN266200700010C
6 · The paper itself

Abstract

The multi-domain non-structural protein 3 of SARS-coronavirus is a component of the viral replication/transcription complex (RTC). Among other domains, it contains three sequentially arranged macrodomains: the X domain and subdomains SUD-N as well as SUD-M within the "SARS-unique domain". The X domain was proposed to be an ADP-ribose-1"-phosphatase or a poly(ADP-ribose)-binding protein, whereas SUD-NM binds oligo(G)-nucleotides capable of forming G-quadruplexes. Here, we describe the application of a reverse genetic approach to assess the importance of these macrodomains for the activity of the SARS-CoV RTC. To this end, Renilla luciferase-encoding SARS-CoV replicons with selectively deleted macrodomains were constructed and their ability to modulate the RTC activity was examined. While the SUD-N and the X domains were found to be dispensable, the SUD-M domain was crucial for viral genome replication/transcription. Moreover, alanine replacement of charged amino-acid residues of the SUD-M domain, which are likely involved in G-quadruplex-binding, caused abrogation of RTC activity.

Indexed as

Transcription, GeneticVirus ReplicationAmino Acid SubstitutionGenes, ReporterLuciferases, RenillaProtein Structure, TertiaryReverse GeneticsSequence DeletionSevere acute respiratory syndrome-related coronavirusStaining and LabelingViral Nonstructural ProteinsLuciferases, RenillaViral Nonstructural ProteinsG-quadruplexMacrodomainMERS-CoVReverse geneticsSARS-CoV repliconSARS-unique domainX-domain

Identifiers

PMID26149721
PMCPMC4567502
OpenAlexW797622151

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.