The envelope protein of severe acute respiratory syndrome coronavirus interacts with the non-structural protein 3 and is ubiquitinated.
Identifieur interne : 002422 ( Main/Exploration ); précédent : 002421; suivant : 002423The envelope protein of severe acute respiratory syndrome coronavirus interacts with the non-structural protein 3 and is ubiquitinated.
Auteurs : Enrique Alvarez [Espagne] ; Marta L. Dediego ; Jose L. Nieto-Torres ; Jose M. Jiménez-Guarde O ; Laura Marcos-Villar ; Luis EnjuanesSource :
- Virology [ 1096-0341 ] ; 2010.
Descripteurs français
- KwdFr :
- Animaux, Cartographie d'interactions entre protéines, Chromatographie d'affinité, Humains, Liaison aux protéines, Lignée cellulaire, Maturation post-traductionnelle des protéines, Motifs et domaines d'intéraction protéique, Protéines de l'enveloppe virale (métabolisme), Protéines virales non structurales (métabolisme), RNA replicase (métabolisme), Ubiquitinylation, Virus du SRAS (physiologie).
- MESH :
- métabolisme : Protéines de l'enveloppe virale, Protéines virales non structurales, RNA replicase.
- physiologie : Virus du SRAS.
- Animaux, Cartographie d'interactions entre protéines, Chromatographie d'affinité, Humains, Liaison aux protéines, Lignée cellulaire, Maturation post-traductionnelle des protéines, Motifs et domaines d'intéraction protéique, Ubiquitinylation.
English descriptors
- KwdEn :
- Animals, Cell Line, Chlorocebus aethiops, Chromatography, Affinity, Humans, Protein Binding, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Protein Processing, Post-Translational, RNA Replicase (metabolism), SARS Virus (physiology), Ubiquitination, Viral Envelope Proteins (metabolism), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , metabolism : RNA Replicase, Viral Envelope Proteins, Viral Nonstructural Proteins.
- physiology : SARS Virus.
- Animals, Cell Line, Chlorocebus aethiops, Chromatography, Affinity, Humans, Protein Binding, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Protein Processing, Post-Translational, Ubiquitination.
Abstract
To analyze the proteins interacting with the severe acute respiratory syndrome coronavirus (SARS-CoV) envelope (E) protein, a SARS-CoV was engineered including two tags associated to the E protein. Using this virus, complexes of SARS-CoV E and other proteins were purified using a tandem affinity purification system. Several viral and cell proteins including spike, membrane, non-structural protein 3 (nsp3), dynein heavy chain, fatty acid synthase and transmembrane protein 43 bound E protein. In the present work, we focused on the binding of E protein to nsp3 in infected cells and cell-free systems. This interaction was mediated by the N-terminal acidic domain of nsp3. Moreover, nsp3 and E protein colocalized during the infection. It was shown that E protein was ubiquitinated in vitro and in cell culture, suggesting that the interaction between nsp3 and E protein may play a role in the E protein ubiquitination status and therefore on its turnover.
DOI: 10.1016/j.virol.2010.03.015
PubMed: 20409569
Affiliations:
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Le document en format XML
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Dediego</name></author><author><name sortKey="Nieto Torres, Jose L" sort="Nieto Torres, Jose L" uniqKey="Nieto Torres J" first="Jose L" last="Nieto-Torres">Jose L. Nieto-Torres</name></author><author><name sortKey="Jimenez Guarde O, Jose M" sort="Jimenez Guarde O, Jose M" uniqKey="Jimenez Guarde O J" first="Jose M" last="Jiménez-Guarde O">Jose M. Jiménez-Guarde O</name></author><author><name sortKey="Marcos Villar, Laura" sort="Marcos Villar, Laura" uniqKey="Marcos Villar L" first="Laura" last="Marcos-Villar">Laura Marcos-Villar</name></author><author><name sortKey="Enjuanes, Luis" sort="Enjuanes, Luis" uniqKey="Enjuanes L" first="Luis" last="Enjuanes">Luis Enjuanes</name></author></analytic><series><title level="j">Virology</title><idno type="eISSN">1096-0341</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Chromatography, Affinity</term><term>Humans</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term><term>Protein Interaction Mapping</term><term>Protein Processing, Post-Translational</term><term>RNA Replicase (metabolism)</term><term>SARS Virus (physiology)</term><term>Ubiquitination</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cartographie d'interactions entre protéines</term><term>Chromatographie d'affinité</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Maturation post-traductionnelle des protéines</term><term>Motifs et domaines d'intéraction protéique</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéines virales non structurales (métabolisme)</term><term>RNA replicase (métabolisme)</term><term>Ubiquitinylation</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA Replicase</term><term>Viral Envelope Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de l'enveloppe virale</term><term>Protéines virales non structurales</term><term>RNA replicase</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Chromatography, Affinity</term><term>Humans</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term><term>Protein Interaction Mapping</term><term>Protein Processing, Post-Translational</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cartographie d'interactions entre protéines</term><term>Chromatographie d'affinité</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Maturation post-traductionnelle des protéines</term><term>Motifs et domaines d'intéraction protéique</term><term>Ubiquitinylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To analyze the proteins interacting with the severe acute respiratory syndrome coronavirus (SARS-CoV) envelope (E) protein, a SARS-CoV was engineered including two tags associated to the E protein. Using this virus, complexes of SARS-CoV E and other proteins were purified using a tandem affinity purification system. Several viral and cell proteins including spike, membrane, non-structural protein 3 (nsp3), dynein heavy chain, fatty acid synthase and transmembrane protein 43 bound E protein. In the present work, we focused on the binding of E protein to nsp3 in infected cells and cell-free systems. This interaction was mediated by the N-terminal acidic domain of nsp3. Moreover, nsp3 and E protein colocalized during the infection. It was shown that E protein was ubiquitinated in vitro and in cell culture, suggesting that the interaction between nsp3 and E protein may play a role in the E protein ubiquitination status and therefore on its turnover.</div></front></TEI><affiliations><list><country><li>Espagne</li></country><region><li>Communauté de Madrid</li></region><settlement><li>Madrid</li></settlement><orgName><li>Université autonome de Madrid</li></orgName></list><tree><noCountry><name sortKey="Dediego, Marta L" sort="Dediego, Marta L" uniqKey="Dediego M" first="Marta L" last="Dediego">Marta L. Dediego</name><name sortKey="Enjuanes, Luis" sort="Enjuanes, Luis" uniqKey="Enjuanes L" first="Luis" last="Enjuanes">Luis Enjuanes</name><name sortKey="Jimenez Guarde O, Jose M" sort="Jimenez Guarde O, Jose M" uniqKey="Jimenez Guarde O J" first="Jose M" last="Jiménez-Guarde O">Jose M. Jiménez-Guarde O</name><name sortKey="Marcos Villar, Laura" sort="Marcos Villar, Laura" uniqKey="Marcos Villar L" first="Laura" last="Marcos-Villar">Laura Marcos-Villar</name><name sortKey="Nieto Torres, Jose L" sort="Nieto Torres, Jose L" uniqKey="Nieto Torres J" first="Jose L" last="Nieto-Torres">Jose L. Nieto-Torres</name></noCountry><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Alvarez, Enrique" sort="Alvarez, Enrique" uniqKey="Alvarez E" first="Enrique" last="Alvarez">Enrique Alvarez</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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