Evidence map›Paper›PMID 35297669›Full record

ArticleJournal of virology2022

Sindbis Macrodomain Poly-ADP-Ribose Hydrolase Activity Is Important for Viral RNA Synthesis.

Eduardo G Aguilar, Gabrielle Paniccia, Carolina Adura, Zakary S Singer, Alison W Ashbrook, Brandon S Razooky, Charles M Rice, Margaret R MacDonald

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
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  6. Mutation of a highly conserved isoleucine residue in loop 2 of severalbioRxiv : the preprint server for biology · 2024
    Article
  7. Article
  8. Review
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

8 authors at 2 institutions in 1 country.

Eduardo G AguilarLaboratory of Virology and Infectious Disease, The Rockefeller Universitygrid.134907.8, New York, New York, USA.
Gabrielle PanicciaLaboratory of Virology and Infectious Disease, The Rockefeller Universitygrid.134907.8, New York, New York, USA.
Carolina AduraHigh-Throughput and Spectroscopy Resource Center, The Rockefeller Universitygrid.134907.8, New York, New York, USA.
Zakary S SingerLaboratory of Virology and Infectious Disease, The Rockefeller Universitygrid.134907.8, New York, New York, USA.
Alison W AshbrookLaboratory of Virology and Infectious Disease, The Rockefeller Universitygrid.134907.8, New York, New York, USA.
Brandon S RazookyLaboratory of Virology and Infectious Disease, The Rockefeller Universitygrid.134907.8, New York, New York, USA.
Charles M RiceLaboratory of Virology and Infectious Disease, The Rockefeller Universitygrid.134907.8, New York, New York, USA.
Margaret R MacDonaldLaboratory of Virology and Infectious Disease, The Rockefeller Universitygrid.134907.8, New York, New York, USA.ORCID 0000-0001-5177-2068
Rockefeller University · USColumbia University · US

Funding

Developing, Demonstrating, and Disseminating Innovative Programs to Achieve Translational SuccessUL1TR001866 · NCATS · ROCKEFELLER UNIVERSITY · PI COLLER, BARRY, KRUEGER, JAMES G · 2016 to 2025
$40.6M
Immunity and Infectious DiseaseT32AI070084 · NIAID · ROCKEFELLER UNIVERSITY · PI Michel C Nussenzweig · 2008 to 2026
$3.3M
ZAP isoforms in innate immunity-the long, the short and the extra-long of it allR01AI114873 · NIAID · ROCKEFELLER UNIVERSITY · PI MACDONALD, MARGARET R · 2015 to 2019
$1.9M
Catching the PARPs: defining the antiviral mechanisms of ADP-ribosylation in SINV infectionF31AI138409 · NIAID · ROCKEFELLER UNIVERSITY · PI AGUILAR, EDUARDO G. · 2018 to 2019
$90k
NCATS NIH HHS UL1 TR001866NIAID NIH HHS F31 AI138409NIAID NIH HHS R01 AI114873NIAID NIH HHS T32 AI070084
6 · The paper itself

Abstract

ADP-ribosylation is a highly dynamic posttranslational modification frequently studied in stress response pathways with recent attention given to its role in response to viral infection. Notably, the alphaviruses encode catalytically active macrodomains capable of ADP-ribosylhydrolase (ARH) activities, implying a role in remodeling the cellular ADP-ribosylome. This report decouples mono- and poly-ARH contributions to macrodomain function using a newly engineered Sindbis virus (SINV) mutant with attenuated poly-ARH activity. Our findings indicate that viral poly-ARH activity is uniquely required for high titer replication in mammalian systems. Despite translating incoming genomic RNA as efficiently as WT virus, mutant viruses have a reduced capacity to establish productive infection, offering a more complete understanding of the kinetics and role of the alphavirus macrodomain with important implications for broader ADP-ribosyltransferase biology.

Indexed as

CoronavirusHydrolasesRNA, ViralSindbis VirusAnimalsMammalsPoly Adenosine Diphosphate RiboseVirus ReplicationHydrolasesPoly Adenosine Diphosphate RiboseRNA, ViralADP-ribosylationalphavirusPARP/ARTDRNA synthesisSindbis virusvirus replication

Identifiers

PMID35297669
PMCPMC9006893
OpenAlexW4220987081

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.