Severe acute respiratory syndrome coronavirus nonstructural protein 2 interacts with a host protein complex involved in mitochondrial biogenesis and intracellular signaling.
Identifieur interne : 001F73 ( Ncbi/Curation ); précédent : 001F72; suivant : 001F74Severe acute respiratory syndrome coronavirus nonstructural protein 2 interacts with a host protein complex involved in mitochondrial biogenesis and intracellular signaling.
Auteurs : Cromwell T. Cornillez-Ty [États-Unis] ; Lujian Liao ; John R. Yates ; Peter Kuhn ; Michael J. BuchmeierSource :
- Journal of virology [ 1098-5514 ] ; 2009.
Descripteurs français
- KwdFr :
- Catalyse, Données de séquences moléculaires, Humains, Liaison aux protéines, Lignée cellulaire, Mitochondries (métabolisme), Protéines de répression (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Structure tertiaire des protéines, Séquence d'acides aminés, Technique de Western, Transcription génétique, Transduction du signal, Virus du SRAS (métabolisme).
- MESH :
- génétique : Protéines virales non structurales.
- métabolisme : Mitochondries, Protéines virales non structurales, Virus du SRAS.
- Catalyse, Données de séquences moléculaires, Humains, Liaison aux protéines, Lignée cellulaire, Protéines de répression, Structure tertiaire des protéines, Séquence d'acides aminés, Technique de Western, Transcription génétique, Transduction du signal.
English descriptors
- KwdEn :
- Amino Acid Sequence, Blotting, Western, Catalysis, Cell Line, Humans, Mitochondria (metabolism), Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Repressor Proteins (chemistry), SARS Virus (metabolism), Signal Transduction, Transcription, Genetic, Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , chemistry : Repressor Proteins.
- chemical , genetics : Viral Nonstructural Proteins.
- metabolism : Mitochondria, SARS Virus, Viral Nonstructural Proteins.
- Amino Acid Sequence, Blotting, Western, Catalysis, Cell Line, Humans, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Signal Transduction, Transcription, Genetic.
Abstract
The severe acute respiratory syndrome coronavirus (SARS-CoV) generates 16 nonstructural proteins (nsp's) through proteolytic cleavage of a large precursor protein. Although several nsp's exhibit catalytic activities that are important for viral replication and transcription, other nsp's have less clearly defined roles during an infection. In order to gain a better understanding of their functions, we attempted to identify host proteins that interact with nsp's during SARS-CoV infections. For nsp2, we identified an interaction with two host proteins, prohibitin 1 (PHB1) and PHB2. Our results suggest that nsp2 may be involved in the disruption of intracellular host signaling during SARS-CoV infections.
DOI: 10.1128/JVI.00842-09
PubMed: 19640993
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pubmed:19640993Le document en format XML
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Torrey Pines Road, La Jolla, California 92037</wicri:regionArea><wicri:noRegion>California 92037</wicri:noRegion></affiliation></author><author><name sortKey="Liao, Lujian" sort="Liao, Lujian" uniqKey="Liao L" first="Lujian" last="Liao">Lujian Liao</name></author><author><name sortKey="Yates, John R" sort="Yates, John R" uniqKey="Yates J" first="John R" last="Yates">John R. Yates</name></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name></author><author><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J" last="Buchmeier">Michael J. 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Cornillez-Ty</name><affiliation wicri:level="1"><nlm:affiliation>Molecular and Integrative Neurosciences Department, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Molecular and Integrative Neurosciences Department, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037</wicri:regionArea><wicri:noRegion>California 92037</wicri:noRegion></affiliation></author><author><name sortKey="Liao, Lujian" sort="Liao, Lujian" uniqKey="Liao L" first="Lujian" last="Liao">Lujian Liao</name></author><author><name sortKey="Yates, John R" sort="Yates, John R" uniqKey="Yates J" first="John R" last="Yates">John R. Yates</name></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name></author><author><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J" last="Buchmeier">Michael J. Buchmeier</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Blotting, Western</term><term>Catalysis</term><term>Cell Line</term><term>Humans</term><term>Mitochondria (metabolism)</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Repressor Proteins (chemistry)</term><term>SARS Virus (metabolism)</term><term>Signal Transduction</term><term>Transcription, Genetic</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Mitochondries (métabolisme)</term><term>Protéines de répression ()</term><term>Protéines virales non structurales (génétique)</term><term>Protéines virales non structurales (métabolisme)</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Technique de Western</term><term>Transcription génétique</term><term>Transduction du signal</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Repressor Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term><term>SARS Virus</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Mitochondries</term><term>Protéines virales non structurales</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Blotting, Western</term><term>Catalysis</term><term>Cell Line</term><term>Humans</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Signal Transduction</term><term>Transcription, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines de répression</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Technique de Western</term><term>Transcription génétique</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) generates 16 nonstructural proteins (nsp's) through proteolytic cleavage of a large precursor protein. Although several nsp's exhibit catalytic activities that are important for viral replication and transcription, other nsp's have less clearly defined roles during an infection. In order to gain a better understanding of their functions, we attempted to identify host proteins that interact with nsp's during SARS-CoV infections. For nsp2, we identified an interaction with two host proteins, prohibitin 1 (PHB1) and PHB2. Our results suggest that nsp2 may be involved in the disruption of intracellular host signaling during SARS-CoV infections.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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