Evidence map›Paper›PMID 32886065›Full record

ArticleeLife2020

Reactive oxygen species oxidize STING and suppress interferon production.

Lili Tao, Andrew Lemoff, Guoxun Wang, Christina Zarek, Alexandria Lowe, Nan Yan, Tiffany A Reese

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

71 citing papers in PubMed, 102 citations in OpenAlex.

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  9. Defective RNA Polymerase III sensing of mitochondrial DNA in pulmonary epithelial cells impairs type I IFN immunity to SARS-CoV-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
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11 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

7 authors at 1 institution in 1 country.

Lili TaoDepartment of Immunology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-9682-3911
Andrew LemoffDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-4943-0170
Guoxun WangDepartment of Immunology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0001-9825-3150
Christina ZarekDepartment of Immunology, University of Texas Southwestern Medical Center, Dallas, United States.
Alexandria LoweDepartment of Immunology, University of Texas Southwestern Medical Center, Dallas, United States.
Nan YanDepartment of Immunology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-0637-3989
Tiffany A ReeseDepartment of Immunology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0003-2325-6546
The University of Texas Southwestern Medical Center · US

Funding

INTEGRATIVE IMMUNOLOGY TRAINING PROGRAMT32AI005284 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI Nan Yan · 2003 to 2026
$7.4M
Defining Mechanisms for Parasite-Driven Effects on Gamma-Herpesvirus LatencyR01AI130020 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI Tiffany Anne Reese · 2018 to 2026
$3.7M
American Heart Association 17SDG33670071Cancer Prevention and Research Institute of Texas RP200118National Institute of Allergy and Infectious Diseases 1R01AI130020-01A1NIAID NIH HHS R01 AI130020NIAID NIH HHS T32 AI005284
6 · The paper itself

Abstract

Reactive oxygen species (ROS) are by-products of cellular respiration that can promote oxidative stress and damage cellular proteins and lipids. One canonical role of ROS is to defend the cell against invading bacterial and viral pathogens. Curiously, some viruses, including herpesviruses, thrive despite the induction of ROS, suggesting that ROS are beneficial for the virus. However, the underlying mechanisms remain unclear. Here, we found that ROS impaired interferon response during murine herpesvirus infection and that the inhibition occurred downstream of cytoplasmic DNA sensing. We further demonstrated that ROS suppressed the type I interferon response by oxidizing Cysteine 147 on murine stimulator of interferon genes (STING), an ER-associated protein that mediates interferon response after cytoplasmic DNA sensing. This inhibited STING polymerization and activation of downstream signaling events. These data indicate that redox regulation of Cysteine 147 of mouse STING, which is equivalent to Cysteine 148 of human STING, controls interferon production. Together, our findings reveal that ROS orchestrates anti-viral immune responses, which can be exploited by viruses to evade cellular defenses.

Indexed as

Immunity, InnateAnimalsAntiviral AgentsCells, CulturedCysteineHerpes SimplexHerpesvirus 1, HumanImmune EvasionInterferon Type IMacrophagesMembrane ProteinsMiceMice, Inbred C57BLReactive Oxygen SpeciesSignal TransductionSTING ProteinAntiviral AgentsCysteineInterferon Type IMembrane ProteinsReactive Oxygen SpeciesSting1 protein, mouseSTING Proteinherpesvirusimmunologyinfectious diseaseinflammationinterferonmicrobiologymousereactive oxygen speciesredox regulationSTING

Identifiers

PMID32886065
PMCPMC7473769
OpenAlexW3083689748

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.