Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein.
Identifieur interne : 003F98 ( Main/Merge ); précédent : 003F97; suivant : 003F99Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein.
Auteurs : Ching-Ping Chan [Hong Kong] ; Kam-Leung Siu ; King-Tung Chin ; Kwok-Yung Yuen ; Bojian Zheng ; Dong-Yan JinSource :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Cellules Vero, Chaperons moléculaires (métabolisme), Dénaturation des protéines, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Humains, Lignée cellulaire, Plasmides (métabolisme), Protéines de l'enveloppe virale (), Protéines du choc thermique (métabolisme), Protéines du choc thermique HSP70 (métabolisme), Protéines liant les séquences stimulatrices de type CCAAT (métabolisme), Protéines membranaires (métabolisme), Réticulum endoplasmique (métabolisme), Virus du SRAS (métabolisme).
- MESH :
- métabolisme : Chaperons moléculaires, Plasmides, Protéines du choc thermique, Protéines du choc thermique HSP70, Protéines liant les séquences stimulatrices de type CCAAT, Protéines membranaires, Réticulum endoplasmique, Virus du SRAS.
- Animaux, Cellules Vero, Dénaturation des protéines, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Lignée cellulaire, Protéines de l'enveloppe virale.
English descriptors
- KwdEn :
- Animals, CCAAT-Enhancer-Binding Proteins (metabolism), Cell Line, Chlorocebus aethiops, Endoplasmic Reticulum (metabolism), HSP70 Heat-Shock Proteins (metabolism), Heat-Shock Proteins (metabolism), Humans, Membrane Glycoproteins (chemistry), Membrane Proteins (metabolism), Molecular Chaperones (metabolism), Plasmids (metabolism), Protein Denaturation, SARS Virus (metabolism), Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (chemistry).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : CCAAT-Enhancer-Binding Proteins, HSP70 Heat-Shock Proteins, Heat-Shock Proteins, Membrane Proteins, Molecular Chaperones.
- metabolism : Endoplasmic Reticulum, Plasmids, SARS Virus.
- Animals, Cell Line, Chlorocebus aethiops, Humans, Protein Denaturation, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
Perturbation of the function of endoplasmic reticulum (ER) causes stress leading to the activation of cell signaling pathways known as the unfolded protein response (UPR). Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) uses ER as a site for synthesis and processing of viral proteins. In this report, we demonstrate that infection with SARS-CoV induces the UPR in cultured cells. A comparison with M, E, and NSP6 proteins indicates that SARS-CoV spike (S) protein sufficiently induces transcriptional activation of several UPR effectors, including glucose-regulated protein 78 (GRP78), GRP94, and C/EBP homologous protein. A substantial amount of S protein accumulates in the ER. The expression of S protein exerts different effects on the three major signaling pathways of the UPR. Particularly, it induces GRP78/94 through PKR-like ER kinase but has no influence on activating transcription factor 6 or X box-binding protein 1. Taken together, our findings suggest that SARS-CoV S protein specifically modulates the UPR to facilitate viral replication.
DOI: 10.1128/JVI.00659-06
PubMed: 16940539
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pubmed:16940539Le document en format XML
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uniqKey="Chin K" first="King-Tung" last="Chin">King-Tung Chin</name></author><author><name sortKey="Yuen, Kwok Yung" sort="Yuen, Kwok Yung" uniqKey="Yuen K" first="Kwok-Yung" last="Yuen">Kwok-Yung Yuen</name></author><author><name sortKey="Zheng, Bojian" sort="Zheng, Bojian" uniqKey="Zheng B" first="Bojian" last="Zheng">Bojian Zheng</name></author><author><name sortKey="Jin, Dong Yan" sort="Jin, Dong Yan" uniqKey="Jin D" first="Dong-Yan" last="Jin">Dong-Yan Jin</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16940539</idno><idno type="pmid">16940539</idno><idno type="doi">10.1128/JVI.00659-06</idno><idno type="wicri:Area/PubMed/Corpus">002111</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002111</idno><idno type="wicri:Area/PubMed/Curation">002111</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002111</idno><idno 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Kong</country><wicri:regionArea>Department of Biochemistry, The University of Hong Kong, 3/F Laboratory Block, Faculty of Medicine Building, 21 Sassoon Road</wicri:regionArea><wicri:noRegion>21 Sassoon Road</wicri:noRegion></affiliation></author><author><name sortKey="Siu, Kam Leung" sort="Siu, Kam Leung" uniqKey="Siu K" first="Kam-Leung" last="Siu">Kam-Leung Siu</name></author><author><name sortKey="Chin, King Tung" sort="Chin, King Tung" uniqKey="Chin K" first="King-Tung" last="Chin">King-Tung Chin</name></author><author><name sortKey="Yuen, Kwok Yung" sort="Yuen, Kwok Yung" uniqKey="Yuen K" first="Kwok-Yung" last="Yuen">Kwok-Yung Yuen</name></author><author><name sortKey="Zheng, Bojian" sort="Zheng, Bojian" uniqKey="Zheng B" first="Bojian" last="Zheng">Bojian Zheng</name></author><author><name sortKey="Jin, Dong Yan" sort="Jin, Dong Yan" uniqKey="Jin D" first="Dong-Yan" last="Jin">Dong-Yan Jin</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>CCAAT-Enhancer-Binding Proteins (metabolism)</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Endoplasmic Reticulum (metabolism)</term><term>HSP70 Heat-Shock Proteins (metabolism)</term><term>Heat-Shock Proteins (metabolism)</term><term>Humans</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Proteins (metabolism)</term><term>Molecular Chaperones (metabolism)</term><term>Plasmids (metabolism)</term><term>Protein Denaturation</term><term>SARS Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Chaperons moléculaires (métabolisme)</term><term>Dénaturation des protéines</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Humains</term><term>Lignée cellulaire</term><term>Plasmides (métabolisme)</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines du choc thermique (métabolisme)</term><term>Protéines du choc thermique HSP70 (métabolisme)</term><term>Protéines liant les séquences stimulatrices de type CCAAT (métabolisme)</term><term>Protéines membranaires (métabolisme)</term><term>Réticulum endoplasmique (métabolisme)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>CCAAT-Enhancer-Binding Proteins</term><term>HSP70 Heat-Shock Proteins</term><term>Heat-Shock Proteins</term><term>Membrane Proteins</term><term>Molecular Chaperones</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endoplasmic Reticulum</term><term>Plasmids</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chaperons moléculaires</term><term>Plasmides</term><term>Protéines du choc thermique</term><term>Protéines du choc thermique HSP70</term><term>Protéines liant les séquences stimulatrices de type CCAAT</term><term>Protéines membranaires</term><term>Réticulum endoplasmique</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Protein Denaturation</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Dénaturation des protéines</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Lignée cellulaire</term><term>Protéines de l'enveloppe virale</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Perturbation of the function of endoplasmic reticulum (ER) causes stress leading to the activation of cell signaling pathways known as the unfolded protein response (UPR). Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) uses ER as a site for synthesis and processing of viral proteins. In this report, we demonstrate that infection with SARS-CoV induces the UPR in cultured cells. A comparison with M, E, and NSP6 proteins indicates that SARS-CoV spike (S) protein sufficiently induces transcriptional activation of several UPR effectors, including glucose-regulated protein 78 (GRP78), GRP94, and C/EBP homologous protein. A substantial amount of S protein accumulates in the ER. The expression of S protein exerts different effects on the three major signaling pathways of the UPR. Particularly, it induces GRP78/94 through PKR-like ER kinase but has no influence on activating transcription factor 6 or X box-binding protein 1. Taken together, our findings suggest that SARS-CoV S protein specifically modulates the UPR to facilitate viral replication.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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