Evidence map›Paper›PMID 35235615›Full record

ArticlePLoS pathogens2022

Kynurenine-3-monooxygenase (KMO) broadly inhibits viral infections via triggering NMDAR/Ca2+ influx and CaMKII/ IRF3-mediated IFN-β production.

Jin Zhao, Jiaoshan Chen, Congcong Wang, Yajie Liu, Minchao Li, Yanjun Li, Ruiting Li, Zirong Han, Junjian Wang, Ling Chen and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 2 pooled it
1.8field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 2 syntheses or guidelines pooled it, 30 citations in OpenAlex.

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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

13 authors at 3 institutions in 2 countries.

Jin ZhaoSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.
Jiaoshan ChenSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.
Congcong WangSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.
Yajie LiuSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.
Minchao LiSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.
Yanjun LiSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.
Ruiting LiSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.
Zirong HanSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.
Junjian WangGuangdong Provincial Key Laboratory of New Drug Design and Evaluation, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, China.
Ling ChenState Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health (GIBH), Chinese Academy of Sciences, Guangzhou, China.ORCID 0000-0003-1485-1626
Yuelong ShuSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.
Genhong ChengDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, California, United States of America.
Caijun SunSchool of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University, Shenzhen, China.ORCID 0000-0002-2000-7053
Sun Yat-sen University · CNChinese Academy of Sciences · CNUniversity of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tryptophan (Trp) metabolism through the kynurenine pathway (KP) is well known to play a critical function in cancer, autoimmune and neurodegenerative diseases. However, its role in host-pathogen interactions has not been characterized yet. Herein, we identified that kynurenine-3-monooxygenase (KMO), a key rate-limiting enzyme in the KP, and quinolinic acid (QUIN), a key enzymatic product of KMO enzyme, exerted a novel antiviral function against a broad range of viruses. Mechanistically, QUIN induced the production of type I interferon (IFN-I) via activating the N-methyl-d-aspartate receptor (NMDAR) and Ca2+ influx to activate Calcium/calmodulin-dependent protein kinase II (CaMKII)/interferon regulatory factor 3 (IRF3). Importantly, QUIN treatment effectively inhibited viral infections and alleviated disease progression in mice. Furthermore, kmo-/- mice were vulnerable to pathogenic viral challenge with severe clinical symptoms. Collectively, our results demonstrated that KMO and its enzymatic product QUIN were potential therapeutics against emerging pathogenic viruses.

Indexed as

Kynurenine 3-MonooxygenaseVirus DiseasesAnimalsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Interferon Regulatory Factor-3KynurenineMiceQuinolinic AcidCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Interferon Regulatory Factor-3Irf3 protein, mouseKynurenineKynurenine 3-MonooxygenaseQuinolinic Acid

Identifiers

PMID35235615
PMCPMC8920235
OpenAlexW4214924084

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.