Evidence map›Paper›PMID 32295917›Full record

ArticleJournal of virology2020

RNase L Amplifies Interferon Signaling by Inducing Protein Kinase R-Mediated Antiviral Stress Granules.

Praveen Manivannan, Mohammad Adnan Siddiqui, Krishnamurthy Malathi

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

52 citing papers in PubMed, 73 citations in OpenAlex.

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  7. RNase L Regulates Antiviral Responsiveness through Cleavage of XBP1 mRNA.bioRxiv : the preprint server for biology · 2026
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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

3 authors at 2 institutions in 1 country.

Praveen ManivannanDepartment of Biological Sciences, University of Toledo, Toledo, Ohio, USA.
Mohammad Adnan SiddiquiDepartment of Medicine, Division of Infectious Diseases, Columbia University Medical Center, New York, New York, USA.
Krishnamurthy MalathiDepartment of Biological Sciences, University of Toledo, Toledo, Ohio, USA Malathi.Krishnamurthy@utoledo.edu.
University of Toledo · USColumbia University Irving Medical Center · US

Funding

Novel role of RNA signaling in cross-talk between autophagy and apoptosisR15AI119980 · NIAID · UNIVERSITY OF TOLEDO · PI KRISHNAMURTHY, MALATHI · 2016 to 2016
$443k
NIAID NIH HHS R15 AI119980
6 · The paper itself

Abstract

Virus infection leads to activation of the interferon (IFN)-induced endoribonuclease RNase L, which results in degradation of viral and cellular RNAs. Both cellular and viral RNA cleavage products of RNase L bind pattern recognition receptors (PRRs), like retinoic acid-inducible I (Rig-I) and melanoma differentiation-associated protein 5 (MDA5), to further amplify IFN production and antiviral response. Although much is known about the mechanics of ligand binding and PRR activation, how cells coordinate RNA sensing with signaling response and interferon production remains unclear. We show that RNA cleavage products of RNase L activity induce the formation of antiviral stress granules (avSGs) by regulating activation of double-stranded RNA (dsRNA)-dependent protein kinase R (PKR) and recruit the antiviral proteins Rig-I, PKR, OAS, and RNase L to avSGs. Biochemical analysis of purified avSGs showed interaction of a key stress granule protein, G3BP1, with only PKR and Rig-I and not with OAS or RNase L. AvSG assembly during RNase L activation is required for IRF3-mediated IFN production, but not IFN signaling or proinflammatory cytokine induction. Consequently, cells lacking avSG formation or RNase L signaling produced less IFN and showed higher susceptibility during Sendai virus infection, demonstrating the importance of avSGs in RNase L-mediated host defense. We propose a role during viral infection for RNase L-cleaved RNAs in inducing avSGs containing antiviral proteins to provide a platform for efficient interaction of RNA ligands with pattern recognition receptors to enhance IFN production to mount an effective antiviral response.

Indexed as

Cell Line, TumorCytoplasmic GranulesDEAD-box RNA HelicasesDNA HelicaseseIF-2 KinaseEndoribonucleasesHumansInterferon-betaInterferonsPoly-ADP-Ribose Binding ProteinsReceptors, Pattern RecognitionRNA, Double-StrandedRNA Recognition Motif ProteinsRNA, ViralSignal Transduction2-5A-dependent ribonucleaseDEAD-box RNA HelicasesDNA HelicasesEIF2AK2 protein, humaneIF-2 KinaseEndoribonucleasesInterferon-betaInterferonsPoly-ADP-Ribose Binding ProteinsReceptors, Pattern RecognitionRNA, Double-StrandedRNA Recognition Motif ProteinsRNA, Viraldouble-stranded RNAinterferonPKRRig-IRNase Lstress granules

Identifiers

PMID32295917
PMCPMC7307175
OpenAlexW3017148855

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.