Evidence map›Paper›PMID 35878012›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

SARS-CoV-2 impairs interferon production via NSP2-induced repression of mRNA translation.

Zhang Xu, Jung-Hyun Choi, David L Dai, Jun Luo, Reese Jalal Ladak, Qian Li, Yimeng Wang, Christine Zhang, Shane Wiebe, Alex C H Liu and 19 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
6.8field-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

49 citing papers in PubMed, 82 citations in OpenAlex.

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  18. A20 as a Potential Therapeutic Target for COVID-19.Immunity, inflammation and disease · 2025
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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

29 authors at 10 institutions in 5 countries.

Zhang XuRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
Jung-Hyun ChoiRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
David L DaiPrincess Margaret Cancer Centre, University Health Network, University of Toronto, Toronto, ON M5G 2C1, Canada.
Jun LuoRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
Reese Jalal LadakRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
Qian LiMeakins-Christie Laboratories and Respiratory Division, McGill University, Montreal, QC, H4A 3J1, Canada.
Yimeng WangLady Davis Institute, Department of Medicine, McGill University, Montreal, QC, H3T 1E2, Canada.
Christine ZhangDepartment of Medical Microbiology, Faculty of Medicine, University of Manitoba, Winnipeg, MB, R3T 2N2, Canada.
Shane WiebeRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
Alex C H LiuPrincess Margaret Cancer Centre, University Health Network, University of Toronto, Toronto, ON M5G 2C1, Canada.
Xiaozhuo RanPrincess Margaret Cancer Centre, University Health Network, University of Toronto, Toronto, ON M5G 2C1, Canada.
Jiaqi YangPrincess Margaret Cancer Centre, University Health Network, University of Toronto, Toronto, ON M5G 2C1, Canada.
Parisa NaeliPatrick G Johnston Centre for Cancer Research, Queen's University Belfast, Belfast, Northern Ireland, BT9 7AE, United Kingdom.
Aitor GarziaLaboratory for RNA Molecular Biology, The Rockefeller University, New York, NY 10065.
Lele ZhouRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
Niaz MahmoodRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
Qiyun DengRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
Mohamed ElaishDepartment of Chemistry, University of Alberta, Edmonton, AB T6G 2G2, Canada.ORCID 0000-0003-3628-5856
Rongtuan LinLady Davis Institute, Department of Medicine, McGill University, Montreal, QC, H3T 1E2, Canada.ORCID 0000-0002-2238-3503
Lara K MahalDepartment of Chemistry, University of Alberta, Edmonton, AB T6G 2G2, Canada.ORCID 0000-0003-4791-8524
Tom C HobmanDepartment of Cell Biology, University of Alberta, Edmonton, AB T6G 2H7, Canada.ORCID 0000-0002-5744-3545
Jerry PelletierRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
Tommy AlainChildren's Hospital of Eastern Ontario Research Institute, Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON, K1H 5B2, Canada.
Silvia M VidalDepartment of Human Genetics, McGill University, Montreal, QC, H3G 0B1 Canada.
Thomas DuchaineRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.
Mohammad T Mazhab-JafariPrincess Margaret Cancer Centre, University Health Network, University of Toronto, Toronto, ON M5G 2C1, Canada.
Xiaojuan MaoDepartment of Medical Microbiology, Faculty of Medicine, University of Manitoba, Winnipeg, MB, R3T 2N2, Canada.
Seyed Mehdi JafarnejadPatrick G Johnston Centre for Cancer Research, Queen's University Belfast, Belfast, Northern Ireland, BT9 7AE, United Kingdom.ORCID 0000-0002-5129-7081
Nahum SonenbergRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, H3A 1A3, Canada.ORCID 0000-0002-4707-8759
McGill University · CAUniversity Health Network · CAQueen's University Belfast · GBUniversity of Alberta · CAUniversity of Manitoba · CACairo University · EGChristie (Canada) · CAMcGill Genome Centre · CARockefeller University · USUniversity of Ottawa · CA

Funding

Biotechnology and Biological Sciences Research Council BB/W008165/1CIHR FDN-148423CIHR MOP-41924
6 · The paper itself

Abstract

Viruses evade the innate immune response by suppressing the production or activity of cytokines such as type I interferons (IFNs). Here we report the discovery of a mechanism by which the SARS-CoV-2 virus coopts an intrinsic cellular machinery to suppress the production of the key immunostimulatory cytokine IFN-β. We reveal that the SARS-CoV-2 encoded nonstructural protein 2 (NSP2) directly interacts with the cellular GIGYF2 protein. This interaction enhances the binding of GIGYF2 to the mRNA cap-binding protein 4EHP, thereby repressing the translation of the

Indexed as

Carrier ProteinsCOVID-19Interferon Type IViral Nonstructural ProteinsCell LineEukaryotic Initiation Factor-4EHumansImmunity, InnateProtein BiosynthesisRNA, MessengerSARS-CoV-2Virus ReplicationCarrier ProteinsEIF4E2 protein, humanEukaryotic Initiation Factor-4EGIGYF2 protein, humanInterferon Type IORF1ab polyprotein, SARS-CoV-2RNA, MessengerViral Nonstructural Proteins4EHPGIGYF2mRNA translationNSP2SARS-CoV-2

Identifiers

PMID35878012
PMCPMC9371684
OpenAlexW4287838589

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.