Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.
Identifieur interne : 001798 ( Main/Exploration ); précédent : 001797; suivant : 001799Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.
Auteurs : Tatiana Fislová [Royaume-Uni] ; Benjamin Thomas ; Katy M. Graef ; Ervin FodorSource :
- Journal of virology [ 1098-5514 ] ; 2010.
Descripteurs français
- KwdFr :
- Chaperonine contenant TCP-1 (), Chaperonine contenant TCP-1 (génétique), Chaperonine contenant TCP-1 (métabolisme), Grippe humaine (génétique), Grippe humaine (métabolisme), Humains, Liaison aux protéines, Lignée cellulaire, Protéines virales (), Protéines virales (génétique), Protéines virales (métabolisme), Sites de fixation, Virus de la grippe A (enzymologie), Virus de la grippe A (génétique), Virus de la grippe A (physiologie).
- MESH :
- enzymologie : Virus de la grippe A.
- génétique : Chaperonine contenant TCP-1, Grippe humaine, Protéines virales, Virus de la grippe A.
- métabolisme : Chaperonine contenant TCP-1, Grippe humaine, Protéines virales.
- physiologie : Virus de la grippe A.
- Chaperonine contenant TCP-1, Humains, Liaison aux protéines, Lignée cellulaire, Protéines virales, Sites de fixation.
English descriptors
- KwdEn :
- Binding Sites, Cell Line, Chaperonin Containing TCP-1 (chemistry), Chaperonin Containing TCP-1 (genetics), Chaperonin Containing TCP-1 (metabolism), Humans, Influenza A virus (enzymology), Influenza A virus (genetics), Influenza A virus (physiology), Influenza, Human (genetics), Influenza, Human (metabolism), Protein Binding, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Chaperonin Containing TCP-1, Viral Proteins.
- chemical , genetics : Chaperonin Containing TCP-1, Viral Proteins.
- chemical , metabolism : Chaperonin Containing TCP-1, Viral Proteins.
- enzymology : Influenza A virus.
- genetics : Influenza A virus, Influenza, Human.
- metabolism : Influenza, Human.
- physiology : Influenza A virus.
- Binding Sites, Cell Line, Humans, Protein Binding.
Abstract
The RNA polymerase of influenza A virus is a host range determinant and virulence factor. In particular, the PB2 subunit of the RNA polymerase has been implicated as a crucial factor that affects cell tropism as well as virulence in animal models. These findings suggest that host factors associating with the PB2 protein may play an important role during viral replication. In order to identify host factors that associate with the PB2 protein, we purified recombinant PB2 from transiently transfected mammalian cells and identified copurifying host proteins by mass spectrometry. We found that the PB2 protein associates with the cytosolic chaperonin containing TCP-1 (CCT), stress-induced phosphoprotein 1 (STIP1), FK506 binding protein 5 (FKBP5), alpha- and beta-tubulin, Hsp60, and mitochondrial protein p32. Some of these binding partners associate with each other, suggesting that PB2 might interact with these proteins in multimeric complexes. More detailed analysis of the interaction of the PB2 protein with CCT revealed that PB2 associates with CCT as a monomer and that the CCT binding site is located in a central region of the PB2 protein. PB2 proteins from various influenza virus subtypes and origins can associate with CCT. Silencing of CCT resulted in reduced viral replication and reduced PB2 protein and viral RNA accumulation in a ribonucleoprotein reconstitution assay, suggesting an important function for CCT during the influenza virus life cycle. We propose that CCT might be acting as a chaperone for PB2 to aid its folding and possibly its incorporation into the trimeric RNA polymerase complex.
DOI: 10.1128/JVI.00813-10
PubMed: 20573828
Affiliations:
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Le document en format XML
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Graef</name></author><author><name sortKey="Fodor, Ervin" sort="Fodor, Ervin" uniqKey="Fodor E" first="Ervin" last="Fodor">Ervin Fodor</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Cell Line</term><term>Chaperonin Containing TCP-1 (chemistry)</term><term>Chaperonin Containing TCP-1 (genetics)</term><term>Chaperonin Containing TCP-1 (metabolism)</term><term>Humans</term><term>Influenza A virus (enzymology)</term><term>Influenza A virus (genetics)</term><term>Influenza A virus (physiology)</term><term>Influenza, Human (genetics)</term><term>Influenza, Human (metabolism)</term><term>Protein Binding</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chaperonine contenant TCP-1 ()</term><term>Chaperonine contenant TCP-1 (génétique)</term><term>Chaperonine contenant TCP-1 (métabolisme)</term><term>Grippe humaine (génétique)</term><term>Grippe humaine (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines virales ()</term><term>Protéines virales (génétique)</term><term>Protéines virales (métabolisme)</term><term>Sites de fixation</term><term>Virus de la grippe A (enzymologie)</term><term>Virus de la grippe A (génétique)</term><term>Virus de la grippe A (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chaperonin Containing TCP-1</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Chaperonin Containing TCP-1</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chaperonin Containing TCP-1</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Influenza A virus</term><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Chaperonine contenant TCP-1</term><term>Grippe humaine</term><term>Protéines virales</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chaperonine contenant TCP-1</term><term>Grippe humaine</term><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Cell Line</term><term>Humans</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chaperonine contenant TCP-1</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines virales</term><term>Sites de fixation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The RNA polymerase of influenza A virus is a host range determinant and virulence factor. In particular, the PB2 subunit of the RNA polymerase has been implicated as a crucial factor that affects cell tropism as well as virulence in animal models. These findings suggest that host factors associating with the PB2 protein may play an important role during viral replication. In order to identify host factors that associate with the PB2 protein, we purified recombinant PB2 from transiently transfected mammalian cells and identified copurifying host proteins by mass spectrometry. We found that the PB2 protein associates with the cytosolic chaperonin containing TCP-1 (CCT), stress-induced phosphoprotein 1 (STIP1), FK506 binding protein 5 (FKBP5), alpha- and beta-tubulin, Hsp60, and mitochondrial protein p32. Some of these binding partners associate with each other, suggesting that PB2 might interact with these proteins in multimeric complexes. More detailed analysis of the interaction of the PB2 protein with CCT revealed that PB2 associates with CCT as a monomer and that the CCT binding site is located in a central region of the PB2 protein. PB2 proteins from various influenza virus subtypes and origins can associate with CCT. Silencing of CCT resulted in reduced viral replication and reduced PB2 protein and viral RNA accumulation in a ribonucleoprotein reconstitution assay, suggesting an important function for CCT during the influenza virus life cycle. We propose that CCT might be acting as a chaperone for PB2 to aid its folding and possibly its incorporation into the trimeric RNA polymerase complex.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Oxfordshire</li></region><settlement><li>Oxford</li></settlement><orgName><li>Université d'Oxford</li></orgName></list><tree><noCountry><name sortKey="Fodor, Ervin" sort="Fodor, Ervin" uniqKey="Fodor E" first="Ervin" last="Fodor">Ervin Fodor</name><name sortKey="Graef, Katy M" sort="Graef, Katy M" uniqKey="Graef K" first="Katy M" last="Graef">Katy M. Graef</name><name sortKey="Thomas, Benjamin" sort="Thomas, Benjamin" uniqKey="Thomas B" first="Benjamin" last="Thomas">Benjamin Thomas</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Fislova, Tatiana" sort="Fislova, Tatiana" uniqKey="Fislova T" first="Tatiana" last="Fislová">Tatiana Fislová</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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