SrasV1, PubMed, Checkpoint, bibRecord, 001790

Severe acute respiratory syndrome coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3.TANK.TBK1/IKKepsilon complex.

Identifieur interne : 001790 ( PubMed/Checkpoint ); précédent : 001789; suivant : 001791

Severe acute respiratory syndrome coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3.TANK.TBK1/IKKepsilon complex.

Auteurs : Kam-Leung Siu [Hong Kong] ; Kin-Hang Kok ; Ming-Him James Ng ; Vincent K M. Poon ; Kwok-Yung Yuen ; Bo-Jian Zheng ; Dong-Yan Jin

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2009.

RBID : pubmed:19380580

Descripteurs français

English descriptors

KwdEn :
- Adaptor Proteins, Signal Transducing (metabolism), Gene Expression Regulation (immunology), HeLa Cells, Humans, I-kappa B Kinase (metabolism), Interferon Regulatory Factor-3 (metabolism), Interferon Type I (genetics), Interferon Type I (immunology), Kidney (cytology), Phosphorylation, Protein-Serine-Threonine Kinases (metabolism), SARS Virus (immunology), Severe Acute Respiratory Syndrome (immunology), Severe Acute Respiratory Syndrome (virology), Signal Transduction (immunology), TNF Receptor-Associated Factor 3 (metabolism), Viral Matrix Proteins (immunology), Viral Matrix Proteins (metabolism).
MESH :
- chemical , genetics : Interferon Type I.
- chemical , immunology : Interferon Type I, Viral Matrix Proteins.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, I-kappa B Kinase, Interferon Regulatory Factor-3, Protein-Serine-Threonine Kinases, TNF Receptor-Associated Factor 3, Viral Matrix Proteins.
- cytology : Kidney.
- immunology : Gene Expression Regulation, SARS Virus, Severe Acute Respiratory Syndrome, Signal Transduction.
- virology : Severe Acute Respiratory Syndrome.
- HeLa Cells, Humans, Phosphorylation.

Abstract

Severe acute respiratory syndrome (SARS) coronavirus is highly pathogenic in humans and evades innate immunity at multiple levels. It has evolved various strategies to counteract the production and action of type I interferons, which mobilize the front-line defense against viral infection. In this study we demonstrate that SARS coronavirus M protein inhibits gene transcription of type I interferons. M protein potently antagonizes the activation of interferon-stimulated response element-dependent transcription by double-stranded RNA, RIG-I, MDA5, TBK1, IKKepsilon, and virus-induced signaling adaptor (VISA) but has no influence on the transcriptional activity of this element when IRF3 or IRF7 is overexpressed. M protein physically associates with RIG-I, TBK1, IKKepsilon, and TRAF3 and likely sequesters some of them in membrane-associated cytoplasmic compartments. Consequently, the expression of M protein prevents the formation of TRAF3.TANK.TBK1/IKKepsilon complex and thereby inhibits TBK1/IKKepsilon-dependent activation of IRF3/IRF7 transcription factors. Taken together, our findings reveal a new mechanism by which SARS coronavirus circumvents the production of type I interferons.

DOI: 10.1074/jbc.M109.008227
PubMed: 19380580

Affiliations:

Hong Kong

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001923
to stream PubMed, to step Curation: 001923

Links to Exploration step

pubmed:19380580

Le document en format XML

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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) coronavirus is highly pathogenic in humans and evades innate immunity at multiple levels. It has evolved various strategies to counteract the production and action of type I interferons, which mobilize the front-line defense against viral infection. In this study we demonstrate that SARS coronavirus M protein inhibits gene transcription of type I interferons. M protein potently antagonizes the activation of interferon-stimulated response element-dependent transcription by double-stranded RNA, RIG-I, MDA5, TBK1, IKKepsilon, and virus-induced signaling adaptor (VISA) but has no influence on the transcriptional activity of this element when IRF3 or IRF7 is overexpressed. M protein physically associates with RIG-I, TBK1, IKKepsilon, and TRAF3 and likely sequesters some of them in membrane-associated cytoplasmic compartments. Consequently, the expression of M protein prevents the formation of TRAF3.TANK.TBK1/IKKepsilon complex and thereby inhibits TBK1/IKKepsilon-dependent activation of IRF3/IRF7 transcription factors. Taken together, our findings reveal a new mechanism by which SARS coronavirus circumvents the production of type I interferons.</div>
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<Abstract><AbstractText>Severe acute respiratory syndrome (SARS) coronavirus is highly pathogenic in humans and evades innate immunity at multiple levels. It has evolved various strategies to counteract the production and action of type I interferons, which mobilize the front-line defense against viral infection. In this study we demonstrate that SARS coronavirus M protein inhibits gene transcription of type I interferons. M protein potently antagonizes the activation of interferon-stimulated response element-dependent transcription by double-stranded RNA, RIG-I, MDA5, TBK1, IKKepsilon, and virus-induced signaling adaptor (VISA) but has no influence on the transcriptional activity of this element when IRF3 or IRF7 is overexpressed. M protein physically associates with RIG-I, TBK1, IKKepsilon, and TRAF3 and likely sequesters some of them in membrane-associated cytoplasmic compartments. Consequently, the expression of M protein prevents the formation of TRAF3.TANK.TBK1/IKKepsilon complex and thereby inhibits TBK1/IKKepsilon-dependent activation of IRF3/IRF7 transcription factors. Taken together, our findings reveal a new mechanism by which SARS coronavirus circumvents the production of type I interferons.</AbstractText>
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Severe acute respiratory syndrome coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3.TANK.TBK1/IKKepsilon complex.

Severe acute respiratory syndrome coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3.TANK.TBK1/IKKepsilon complex.

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