Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus.
Identifieur interne : 001D36 ( PubMed/Curation ); précédent : 001D35; suivant : 001D37Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus.
Auteurs : Santhana G. Devaraj [États-Unis] ; Nan Wang ; Zhongbin Chen ; Zihong Chen ; Monica Tseng ; Naina Barretto ; Rongtuan Lin ; Clarence J. Peters ; Chien-Te K. Tseng ; Susan C. Baker ; Kui LiSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux, Bronches (cytologie), Bronches (immunologie), Bronches (virologie), Facteur-3 de régulation d'interféron (immunologie), Humains, Immunité innée, Interféron de type I (immunologie), Lignée cellulaire, Peptide hydrolases (), Peptide hydrolases (immunologie), Protéines virales (), Protéines virales (immunologie), Structure tertiaire des protéines, Syndrome respiratoire aigu sévère (immunologie), Syndrome respiratoire aigu sévère (virologie), Virus du SRAS (enzymologie), Virus du SRAS (immunologie).
- MESH :
- cytologie : Bronches.
- enzymologie : Virus du SRAS.
- immunologie : Bronches, Facteur-3 de régulation d'interféron, Interféron de type I, Peptide hydrolases, Protéines virales, Syndrome respiratoire aigu sévère, Virus du SRAS.
- virologie : Bronches, Syndrome respiratoire aigu sévère.
- Animaux, Humains, Immunité innée, Lignée cellulaire, Peptide hydrolases, Protéines virales, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Animals, Bronchi (cytology), Bronchi (immunology), Bronchi (virology), Cell Line, Humans, Immunity, Innate, Interferon Regulatory Factor-3 (immunology), Interferon Type I (immunology), Peptide Hydrolases (chemistry), Peptide Hydrolases (immunology), Protein Structure, Tertiary, SARS Virus (enzymology), SARS Virus (immunology), Severe Acute Respiratory Syndrome (immunology), Severe Acute Respiratory Syndrome (virology), Viral Proteins (chemistry), Viral Proteins (immunology).
- MESH :
- chemical , chemistry : Peptide Hydrolases, Viral Proteins.
- chemical , immunology : Interferon Regulatory Factor-3, Interferon Type I, Peptide Hydrolases, Viral Proteins.
- cytology : Bronchi.
- enzymology : SARS Virus.
- immunology : Bronchi, SARS Virus, Severe Acute Respiratory Syndrome.
- virology : Bronchi, Severe Acute Respiratory Syndrome.
- Animals, Cell Line, Humans, Immunity, Innate, Protein Structure, Tertiary.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) is a novel coronavirus that causes a highly contagious respiratory disease, SARS, with significant mortality. Although factors contributing to the highly pathogenic nature of SARS-CoV remain poorly understood, it has been reported that SARS-CoV infection does not induce type I interferons (IFNs) in cell culture. However, it is uncertain whether SARS-CoV evades host detection or has evolved mechanisms to counteract innate host defenses. We show here that infection of SARS-CoV triggers a weak IFN response in cultured human lung/bronchial epithelial cells without inducing the phosphorylation of IFN-regulatory factor 3 (IRF-3), a latent cellular transcription factor that is pivotal for type I IFN synthesis. Furthermore, SARS-CoV infection blocked the induction of IFN antiviral activity and the up-regulation of protein expression of a subset of IFN-stimulated genes triggered by double-stranded RNA or an unrelated paramyxovirus. In searching for a SARS-CoV protein capable of counteracting innate immunity, we identified the papain-like protease (PLpro) domain as a potent IFN antagonist. The inhibition of the IFN response does not require the protease activity of PLpro. Rather, PLpro interacts with IRF-3 and inhibits the phosphorylation and nuclear translocation of IRF-3, thereby disrupting the activation of type I IFN responses through either Toll-like receptor 3 or retinoic acid-inducible gene I/melanoma differentiation-associated gene 5 pathways. Our data suggest that regulation of IRF-3-dependent innate antiviral defenses by PLpro may contribute to the establishment of SARS-CoV infection.
DOI: 10.1074/jbc.M704870200
PubMed: 17761676
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pubmed:17761676Le document en format XML
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) is a novel coronavirus that causes a highly contagious respiratory disease, SARS, with significant mortality. Although factors contributing to the highly pathogenic nature of SARS-CoV remain poorly understood, it has been reported that SARS-CoV infection does not induce type I interferons (IFNs) in cell culture. However, it is uncertain whether SARS-CoV evades host detection or has evolved mechanisms to counteract innate host defenses. We show here that infection of SARS-CoV triggers a weak IFN response in cultured human lung/bronchial epithelial cells without inducing the phosphorylation of IFN-regulatory factor 3 (IRF-3), a latent cellular transcription factor that is pivotal for type I IFN synthesis. Furthermore, SARS-CoV infection blocked the induction of IFN antiviral activity and the up-regulation of protein expression of a subset of IFN-stimulated genes triggered by double-stranded RNA or an unrelated paramyxovirus. In searching for a SARS-CoV protein capable of counteracting innate immunity, we identified the papain-like protease (PLpro) domain as a potent IFN antagonist. The inhibition of the IFN response does not require the protease activity of PLpro. Rather, PLpro interacts with IRF-3 and inhibits the phosphorylation and nuclear translocation of IRF-3, thereby disrupting the activation of type I IFN responses through either Toll-like receptor 3 or retinoic acid-inducible gene I/melanoma differentiation-associated gene 5 pathways. Our data suggest that regulation of IRF-3-dependent innate antiviral defenses by PLpro may contribute to the establishment of SARS-CoV infection.</div>
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<Abstract><AbstractText>Severe acute respiratory syndrome coronavirus (SARS-CoV) is a novel coronavirus that causes a highly contagious respiratory disease, SARS, with significant mortality. Although factors contributing to the highly pathogenic nature of SARS-CoV remain poorly understood, it has been reported that SARS-CoV infection does not induce type I interferons (IFNs) in cell culture. However, it is uncertain whether SARS-CoV evades host detection or has evolved mechanisms to counteract innate host defenses. We show here that infection of SARS-CoV triggers a weak IFN response in cultured human lung/bronchial epithelial cells without inducing the phosphorylation of IFN-regulatory factor 3 (IRF-3), a latent cellular transcription factor that is pivotal for type I IFN synthesis. Furthermore, SARS-CoV infection blocked the induction of IFN antiviral activity and the up-regulation of protein expression of a subset of IFN-stimulated genes triggered by double-stranded RNA or an unrelated paramyxovirus. In searching for a SARS-CoV protein capable of counteracting innate immunity, we identified the papain-like protease (PLpro) domain as a potent IFN antagonist. The inhibition of the IFN response does not require the protease activity of PLpro. Rather, PLpro interacts with IRF-3 and inhibits the phosphorylation and nuclear translocation of IRF-3, thereby disrupting the activation of type I IFN responses through either Toll-like receptor 3 or retinoic acid-inducible gene I/melanoma differentiation-associated gene 5 pathways. Our data suggest that regulation of IRF-3-dependent innate antiviral defenses by PLpro may contribute to the establishment of SARS-CoV infection.</AbstractText>
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