Evidence map›Paper›PMID 38423012›Full record

ArticleImmunity2024

Oligoadenylate synthetase 1 displays dual antiviral mechanisms in driving translational shutdown and protecting interferon production.

Munesh K Harioudh, Joseph Perez, Zhenlu Chong, Sharmila Nair, Lomon So, Kevin D McCormick, Arundhati Ghosh, Lulu Shao, Rashmi Srivastava, Frank Soveg and 6 more

Open access · greenAbstract read
In one paragraph

Article in Immunity, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
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  9. Journal of virology · 2026
    Article
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  11. iScience · 2025
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 5 institutions in 2 countries.

Munesh K HarioudhCancer Virology Program, UPMC Hillman Cancer Center, Pittsburgh, PA, USA; Department of Microbiology and Molecular Genetics, Pittsburgh, PA, USA.
Joseph PerezCancer Virology Program, UPMC Hillman Cancer Center, Pittsburgh, PA, USA; Department of Microbiology and Molecular Genetics, Pittsburgh, PA, USA.
Zhenlu ChongDepartments of Medicine, Molecular Microbiology, Pathology & Immunology, Washington University School of Medicine, St. Louis, MO, USA.
Sharmila NairDepartments of Medicine, Molecular Microbiology, Pathology & Immunology, Washington University School of Medicine, St. Louis, MO, USA.
Lomon SoDepartment of Immunology, School of Medicine, University of Washington, Seattle, WA, USA; Division of Immunology, Benaroya Research Institute, Seattle, WA, USA.
Kevin D McCormickCancer Virology Program, UPMC Hillman Cancer Center, Pittsburgh, PA, USA; Department of Microbiology and Molecular Genetics, Pittsburgh, PA, USA.
Arundhati GhoshCancer Virology Program, UPMC Hillman Cancer Center, Pittsburgh, PA, USA; Department of Microbiology and Molecular Genetics, Pittsburgh, PA, USA.
Lulu ShaoCancer Virology Program, UPMC Hillman Cancer Center, Pittsburgh, PA, USA; Department of Microbiology and Molecular Genetics, Pittsburgh, PA, USA.
Rashmi SrivastavaCancer Virology Program, UPMC Hillman Cancer Center, Pittsburgh, PA, USA; Department of Microbiology and Molecular Genetics, Pittsburgh, PA, USA.
Frank SovegDepartment of Immunology, School of Medicine, University of Washington, Seattle, WA, USA.
Thomas S EbertDepartment of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Maninjay K AtianandDepartment of Immunology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Veit HornungDepartment of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Ram SavanDepartment of Immunology, School of Medicine, University of Washington, Seattle, WA, USA.
Michael S DiamondDepartments of Medicine, Molecular Microbiology, Pathology & Immunology, Washington University School of Medicine, St. Louis, MO, USA.
Saumendra N SarkarCancer Virology Program, UPMC Hillman Cancer Center, Pittsburgh, PA, USA; Department of Microbiology and Molecular Genetics, Pittsburgh, PA, USA; Department of Immunology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA. Electronic address: saumen@pitt.edu.
UPMC Hillman Cancer Center · USUniversity of Washington · USWashington University in St. Louis · USLudwig-Maximilians-Universität München · DEUniversity of Pittsburgh · US

Funding

VECTOR CORE FACILITYP30CA047904 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CHRISTOPHER J. BAKKENIST · 1988 to 2026
$158.0M
A new mechanism of antiviral activity of 2’-5’ Oligoadenylate Synthetase 1R01AI150214 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI DIAMOND, MICHAEL S, SARKAR, SAUMENDRA N · 2020 to 2024
$2.6M
New roles of IFN-inducible OAS proteins in innate immune defense against bacterial infectionsR01AI176333 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Vijay Rathinam, Saumendra N Sarkar · 2023 to 2026
$2.5M
Differential modulation of RIG-I and cGAS signaling by OASL and its role in antiviral response.R01AI118896 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SARKAR, SAUMENDRA N · 2015 to 2019
$2.1M
NCI NIH HHS P30 CA047904NIAID NIH HHS R01 AI118896NIAID NIH HHS R01 AI150214NIAID NIH HHS R01 AI176333
6 · The paper itself

Abstract

In response to viral infection, how cells balance translational shutdown to limit viral replication and the induction of antiviral components like interferons (IFNs) is not well understood. Moreover, how distinct isoforms of IFN-induced oligoadenylate synthetase 1 (OAS1) contribute to this antiviral response also requires further elucidation. Here, we show that human, but not mouse, OAS1 inhibits SARS-CoV-2 replication through its canonical enzyme activity via RNase L. In contrast, both mouse and human OAS1 protect against West Nile virus infection by a mechanism distinct from canonical RNase L activation. OAS1 binds AU-rich elements (AREs) of specific mRNAs, including IFNβ. This binding leads to the sequestration of IFNβ mRNA to the endomembrane regions, resulting in prolonged half-life and continued translation. Thus, OAS1 is an ARE-binding protein with two mechanisms of antiviral activity: driving inhibition of translation but also a broader, non-canonical function of protecting IFN expression from translational shutdown.

Indexed as

2',5'-Oligoadenylate SynthetaseInterferonsOligoribonucleotidesVirus DiseasesWest Nile FeverAdenine NucleotidesAnimalsAntiviral AgentsHumansMiceWest Nile virus2',5'-oligoadenylate2',5'-Oligoadenylate SynthetaseAdenine NucleotidesAntiviral AgentsInterferonsOas1b protein, mouseOAS1 protein, humanOligoribonucleotidesantiviral mechanisminterferoninterferon-stimulated genesoligoadenylate synthetaseSARS-CoV-2West Nile virus

Identifiers

PMID38423012
PMCPMC10939734
OpenAlexW4392246254

What OpenQuestion holds

Textmetadata
LicenceTDM
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.