A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein.
Identifieur interne : 002B93 ( Main/Exploration ); précédent : 002B92; suivant : 002B94A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein.
Auteurs : Wataru Kamitani [États-Unis] ; Cheng Huang ; Krishna Narayanan ; Kumari G. Lokugamage ; Shinji MakinoSource :
- Nature structural & molecular biology [ 1545-9985 ] ; 2009.
Descripteurs français
- KwdFr :
- Biosynthèse des protéines (), Biosynthèse des protéines (génétique), Humains, Immunoprécipitation, Liaison aux protéines, Lignée cellulaire, Luciférases de Renilla (génétique), Luciférases de Renilla (métabolisme), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Protéines virales non structurales (pharmacologie), Protéines virales non structurales (physiologie), RNA replicase (génétique), RNA replicase (métabolisme), RNA replicase (pharmacologie), RNA replicase (physiologie), Ribosomes (métabolisme), Stabilité de l'ARN.
- MESH :
- génétique : Biosynthèse des protéines, Luciférases de Renilla, Protéines virales non structurales, RNA replicase.
- métabolisme : Luciférases de Renilla, Protéines virales non structurales, RNA replicase, Ribosomes.
- pharmacologie : Protéines virales non structurales, RNA replicase.
- physiologie : Protéines virales non structurales, RNA replicase.
- Biosynthèse des protéines, Humains, Immunoprécipitation, Liaison aux protéines, Lignée cellulaire, Stabilité de l'ARN.
English descriptors
- KwdEn :
- Cell Line, Humans, Immunoprecipitation, Luciferases, Renilla (genetics), Luciferases, Renilla (metabolism), Protein Binding, Protein Biosynthesis (drug effects), Protein Biosynthesis (genetics), RNA Replicase (genetics), RNA Replicase (metabolism), RNA Replicase (pharmacology), RNA Replicase (physiology), RNA Stability, Ribosomes (metabolism), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Viral Nonstructural Proteins (pharmacology), Viral Nonstructural Proteins (physiology).
- MESH :
- chemical , genetics : Luciferases, Renilla, RNA Replicase, Viral Nonstructural Proteins.
- chemical , metabolism : Luciferases, Renilla, RNA Replicase, Viral Nonstructural Proteins.
- drug effects : Protein Biosynthesis.
- genetics : Protein Biosynthesis.
- metabolism : Ribosomes.
- chemical , pharmacology : RNA Replicase, Viral Nonstructural Proteins.
- chemical , physiology : RNA Replicase, Viral Nonstructural Proteins.
- Cell Line, Humans, Immunoprecipitation, Protein Binding, RNA Stability.
Abstract
Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression, including type I interferon production, by promoting host mRNA degradation and inhibiting host translation, in infected cells. We present evidence that nsp1 uses a novel, two-pronged strategy to inhibit host translation and gene expression. Nsp1 bound to the 40S ribosomal subunit and inactivated the translational activity of the 40S subunits. Furthermore, the nsp1-40S ribosome complex induced the modification of the 5' region of capped mRNA template and rendered the template RNA translationally incompetent. Nsp1 also induced RNA cleavage in templates carrying the internal ribosome entry site (IRES) from encephalomyocarditis virus, but not in those carrying IRES elements from hepatitis C or cricket paralysis viruses, demonstrating that the nsp1-induced RNA modification was template-dependent. We speculate that the mRNAs that underwent the nsp1-mediated modification are marked for rapid turnover by the host RNA degradation machinery.
DOI: 10.1038/nsmb.1680
PubMed: 19838190
Affiliations:
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Le document en format XML
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Lokugamage</name></author><author><name sortKey="Makino, Shinji" sort="Makino, Shinji" uniqKey="Makino S" first="Shinji" last="Makino">Shinji Makino</name></author></analytic><series><title level="j">Nature structural & molecular biology</title><idno type="eISSN">1545-9985</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Immunoprecipitation</term><term>Luciferases, Renilla (genetics)</term><term>Luciferases, Renilla (metabolism)</term><term>Protein Binding</term><term>Protein Biosynthesis (drug effects)</term><term>Protein Biosynthesis (genetics)</term><term>RNA Replicase (genetics)</term><term>RNA Replicase (metabolism)</term><term>RNA Replicase (pharmacology)</term><term>RNA Replicase (physiology)</term><term>RNA Stability</term><term>Ribosomes (metabolism)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (metabolism)</term><term>Viral Nonstructural Proteins (pharmacology)</term><term>Viral Nonstructural Proteins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biosynthèse des protéines ()</term><term>Biosynthèse des protéines (génétique)</term><term>Humains</term><term>Immunoprécipitation</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Luciférases de Renilla (génétique)</term><term>Luciférases de Renilla (métabolisme)</term><term>Protéines virales non structurales (génétique)</term><term>Protéines virales non structurales (métabolisme)</term><term>Protéines virales non structurales (pharmacologie)</term><term>Protéines virales non structurales (physiologie)</term><term>RNA replicase (génétique)</term><term>RNA replicase (métabolisme)</term><term>RNA replicase (pharmacologie)</term><term>RNA replicase (physiologie)</term><term>Ribosomes (métabolisme)</term><term>Stabilité de l'ARN</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Luciferases, Renilla</term><term>RNA Replicase</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Luciferases, Renilla</term><term>RNA Replicase</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Protein Biosynthesis</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Protein Biosynthesis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Biosynthèse des protéines</term><term>Luciférases de Renilla</term><term>Protéines virales non structurales</term><term>RNA replicase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Ribosomes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Luciférases de Renilla</term><term>Protéines virales non structurales</term><term>RNA replicase</term><term>Ribosomes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Protéines virales non structurales</term><term>RNA replicase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>RNA Replicase</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines virales non structurales</term><term>RNA replicase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>RNA Replicase</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Immunoprecipitation</term><term>Protein Binding</term><term>RNA Stability</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biosynthèse des protéines</term><term>Humains</term><term>Immunoprécipitation</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Stabilité de l'ARN</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression, including type I interferon production, by promoting host mRNA degradation and inhibiting host translation, in infected cells. We present evidence that nsp1 uses a novel, two-pronged strategy to inhibit host translation and gene expression. Nsp1 bound to the 40S ribosomal subunit and inactivated the translational activity of the 40S subunits. Furthermore, the nsp1-40S ribosome complex induced the modification of the 5' region of capped mRNA template and rendered the template RNA translationally incompetent. Nsp1 also induced RNA cleavage in templates carrying the internal ribosome entry site (IRES) from encephalomyocarditis virus, but not in those carrying IRES elements from hepatitis C or cricket paralysis viruses, demonstrating that the nsp1-induced RNA modification was template-dependent. We speculate that the mRNAs that underwent the nsp1-mediated modification are marked for rapid turnover by the host RNA degradation machinery.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Texas</li></region></list><tree><noCountry><name sortKey="Huang, Cheng" sort="Huang, Cheng" uniqKey="Huang C" first="Cheng" last="Huang">Cheng Huang</name><name sortKey="Lokugamage, Kumari G" sort="Lokugamage, Kumari G" uniqKey="Lokugamage K" first="Kumari G" last="Lokugamage">Kumari G. Lokugamage</name><name sortKey="Makino, Shinji" sort="Makino, Shinji" uniqKey="Makino S" first="Shinji" last="Makino">Shinji Makino</name><name sortKey="Narayanan, Krishna" sort="Narayanan, Krishna" uniqKey="Narayanan K" first="Krishna" last="Narayanan">Krishna Narayanan</name></noCountry><country name="États-Unis"><region name="Texas"><name sortKey="Kamitani, Wataru" sort="Kamitani, Wataru" uniqKey="Kamitani W" first="Wataru" last="Kamitani">Wataru Kamitani</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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