StressCovidV1, PubMed, Checkpoint, bibRecord, 000240

The RNA Helicase DDX6 Associates with RIG-I to Augment Induction of Antiviral Signaling.

Identifieur interne : 000240 ( PubMed/Checkpoint ); précédent : 000239; suivant : 000241

The RNA Helicase DDX6 Associates with RIG-I to Augment Induction of Antiviral Signaling.

Auteurs : Rocío Davi A Nú Ez [Allemagne] ; Matthias Budt [Allemagne] ; Sandra Saenger [Allemagne] ; Katharina Paki [Allemagne] ; Ulrike Arnold [Allemagne] ; Anne Sadewasser [Allemagne] ; Thorsten Wolff [Allemagne]

Source :

International journal of molecular sciences [ 1422-0067 ] ; 2018.

RBID : pubmed:29949917

Descripteurs français

English descriptors

KwdEn :
- A549 Cells, Antiviral Agents (metabolism), Cytoplasmic Granules (metabolism), DEAD Box Protein 58 (chemistry), DEAD Box Protein 58 (metabolism), DEAD-box RNA Helicases (metabolism), Gene Expression Regulation, HeLa Cells, Humans, Interferon-beta (genetics), Interferon-beta (metabolism), Protein Binding, Protein Domains, Protein Transport, Proto-Oncogene Proteins (metabolism), RNA, Viral (metabolism), Signal Transduction.
MESH :
- chemical , chemistry : DEAD Box Protein 58.
- chemical , genetics : Interferon-beta.
- chemical , metabolism : Antiviral Agents, DEAD Box Protein 58, DEAD-box RNA Helicases, Interferon-beta, Proto-Oncogene Proteins, RNA, Viral.
- metabolism : Cytoplasmic Granules.
- A549 Cells, Gene Expression Regulation, HeLa Cells, Humans, Protein Binding, Protein Domains, Protein Transport, Signal Transduction.

Abstract

Virus infections induce sensitive antiviral responses within the host cell. The RNA helicase retinoic acid-inducible gene I (RIG-I) is a key sensor of influenza virus RNA that induces the expression of antiviral type I interferons. Recent evidence suggests a complex pattern of RIG-I regulation involving multiple interactions and cellular sites. In an approach employing affinity purification and quantitative mass spectrometry, we identified proteins with increased binding to RIG-I in response to influenza B virus infection. Among them was the RIG-I related RNA helicase DEAD box helicase 6 (DDX6), a known component of cytoplasmic mRNA-ribonucleoprotein (mRNP) granules like P-bodies and stress granules (SGs). RIG-I and DDX6 both localized to the cytosol and were detected in virus-induced SGs. Coimmunoprecipitation assays detected a basal level of complexes harboring RIG-I and DDX6 that increased after infection. Functionally, DDX6 augmented RIG-I mediated induction of interferon (IFN)-β expression. Notably, DDX6 was found to bind viral RNA capable to stimulate RIG-I. These findings imply a novel function for DDX6 as an RNA co-sensor and signaling enhancer for RIG-I.

DOI: 10.3390/ijms19071877
PubMed: 29949917

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Virus infections induce sensitive antiviral responses within the host cell. The RNA helicase retinoic acid-inducible gene I (RIG-I) is a key sensor of influenza virus RNA that induces the expression of antiviral type I interferons. Recent evidence suggests a complex pattern of RIG-I regulation involving multiple interactions and cellular sites. In an approach employing affinity purification and quantitative mass spectrometry, we identified proteins with increased binding to RIG-I in response to influenza B virus infection. Among them was the RIG-I related RNA helicase DEAD box helicase 6 (DDX6), a known component of cytoplasmic mRNA-ribonucleoprotein (mRNP) granules like P-bodies and stress granules (SGs). RIG-I and DDX6 both localized to the cytosol and were detected in virus-induced SGs. Coimmunoprecipitation assays detected a basal level of complexes harboring RIG-I and DDX6 that increased after infection. Functionally, DDX6 augmented RIG-I mediated induction of interferon (IFN)-β expression. Notably, DDX6 was found to bind viral RNA capable to stimulate RIG-I. These findings imply a novel function for DDX6 as an RNA co-sensor and signaling enhancer for RIG-I.</div>
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<Abstract><AbstractText>Virus infections induce sensitive antiviral responses within the host cell. The RNA helicase retinoic acid-inducible gene I (RIG-I) is a key sensor of influenza virus RNA that induces the expression of antiviral type I interferons. Recent evidence suggests a complex pattern of RIG-I regulation involving multiple interactions and cellular sites. In an approach employing affinity purification and quantitative mass spectrometry, we identified proteins with increased binding to RIG-I in response to influenza B virus infection. Among them was the RIG-I related RNA helicase DEAD box helicase 6 (DDX6), a known component of cytoplasmic mRNA-ribonucleoprotein (mRNP) granules like P-bodies and stress granules (SGs). RIG-I and DDX6 both localized to the cytosol and were detected in virus-induced SGs. Coimmunoprecipitation assays detected a basal level of complexes harboring RIG-I and DDX6 that increased after infection. Functionally, DDX6 augmented RIG-I mediated induction of interferon (IFN)-β expression. Notably, DDX6 was found to bind viral RNA capable to stimulate RIG-I. These findings imply a novel function for DDX6 as an RNA co-sensor and signaling enhancer for RIG-I.</AbstractText>
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The RNA Helicase DDX6 Associates with RIG-I to Augment Induction of Antiviral Signaling.

The RNA Helicase DDX6 Associates with RIG-I to Augment Induction of Antiviral Signaling.

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