Evidence map›Paper›PMID 32198201›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Coronavirus endoribonuclease targets viral polyuridine sequences to evade activating host sensors.

Matthew Hackbart, Xufang Deng, Susan C Baker

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 199 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
199citing papers in PubMed, 3 pooled it
6.4field-weighted citation impact, top 3% 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

199 citing papers in PubMed, 3 syntheses or guidelines pooled it, 309 citations in OpenAlex.

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  18. Mutant p53 binds RNA to drive mitochondrial dysfunction.bioRxiv : the preprint server for biology · 2025
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139 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

3 authors at 1 institution in 1 country.

Matthew HackbartDepartment of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL 60153.ORCID 0000-0001-6244-6292
Xufang DengDepartment of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL 60153.ORCID 0000-0002-7604-3627
Susan C BakerDepartment of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL 60153 sbaker1@luc.edu.
Loyola University Chicago · US

Funding

Mechanisms of viral proteases in coronavirus replication and pathogenesisR01AI085089 · NIAID · LOYOLA UNIVERSITY CHICAGO · PI BAKER, SUSAN C., MESECAR, ANDREW D · 2010 to 2019
$6.8M
Experimental Immunology Training GrantT32AI007508 · NIAID · LOYOLA UNIVERSITY CHICAGO · PI KNIGHT, KATHERINE L. · 1997 to 2022
$4.0M
NIAID NIH HHS R01 AI085089NIAID NIH HHS T32 AI007508
6 · The paper itself

Abstract

Coronaviruses (CoVs) are positive-sense RNA viruses that can emerge from endemic reservoirs and infect zoonotically, causing significant morbidity and mortality. CoVs encode an endoribonuclease designated EndoU that facilitates evasion of host pattern recognition receptor MDA5, but the target of EndoU activity was not known. Here, we report that EndoU cleaves the 5'-polyuridines from negative-sense viral RNA, termed PUN RNA, which is the product of polyA-templated RNA synthesis. Using a virus containing an EndoU catalytic-inactive mutation, we detected a higher abundance of PUN RNA in the cytoplasm compared to wild-type-infected cells. Furthermore, we found that transfecting PUN RNA into cells stimulates a robust, MDA5-dependent interferon response, and that removal of the polyuridine extension on the RNA dampens the response. Overall, the results of this study reveal the PUN RNA to be a CoV MDA5-dependent pathogen-associated molecular pattern (PAMP). We also establish a mechanism for EndoU activity to cleave and limit the accumulation of this PAMP. Since EndoU activity is highly conserved in all CoVs, inhibiting this activity may serve as an approach for therapeutic interventions against existing and emerging CoV infections.

Indexed as

AnimalsAntiviral AgentsCell LineChlorocebus aethiopsCoronavirusCoronavirus InfectionsEndoribonucleasesHost Microbial InteractionsHumansInterferonsPoly URNA, ViralUridineVero CellsViral Nonstructural ProteinsVirus ReplicationAntiviral AgentsEndoribonucleasesInterferonsnidoviral uridylate-specific endoribonucleasePoly URNA, ViralUridineViral Nonstructural ProteinscoronavirusendoribonucleaseEndoUinterferonnsp15

Identifiers

PMID32198201
PMCPMC7149396
OpenAlexW3011416532

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.