Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein
Identifieur interne : 004432 ( Main/Exploration ); précédent : 004431; suivant : 004433Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein
Auteurs : Ching-Ping Chan [Hong Kong] ; Kam-Leung Siu [Hong Kong] ; King-Tung Chin [Hong Kong] ; Kwok-Yung Yuen [Hong Kong] ; BOJIAN ZHENG [Hong Kong] ; Dong-Yan Jin [Hong Kong]Source :
- 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 :
- Pascal (Inist)
English descriptors
- KwdEn :
- Animals, CCAAT-Enhancer-Binding Proteins (metabolism), Cell Line, Chlorocebus aethiops, Coronavirus, Endoplasmic Reticulum (metabolism), HSP70 Heat-Shock Proteins (metabolism), Heat-Shock Proteins (metabolism), Humans, Membrane Glycoproteins (chemistry), Membrane Proteins (metabolism), Microbiology, Molecular Chaperones (metabolism), Plasmids (metabolism), Protein, Protein Denaturation, SARS Virus (metabolism), Severe acute respiratory syndrome, Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (chemistry), Virology.
- 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.
Affiliations:
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aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Hong Kong</country><wicri:noRegion>Department of Biochemistry, The University of Hong Kong</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><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Biochemistry, The University of Hong Kong</s1><s3>HKG</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Hong Kong</country><wicri:noRegion>Department of Biochemistry, The University of Hong Kong</wicri:noRegion></affiliation></author><author><name sortKey="Chin, King Tung" sort="Chin, King Tung" uniqKey="Chin K" first="King-Tung" last="Chin">King-Tung Chin</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Biochemistry, The University of Hong Kong</s1><s3>HKG</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Hong Kong</country><wicri:noRegion>Department of Biochemistry, The University of Hong Kong</wicri:noRegion></affiliation></author><author><name sortKey="Yuen, Kwok Yung" sort="Yuen, Kwok Yung" uniqKey="Yuen K" first="Kwok-Yung" last="Yuen">Kwok-Yung Yuen</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Microbiology, The University of Hong Kong</s1><s3>HKG</s3><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Hong Kong</country><wicri:noRegion>Department of Microbiology, The University of Hong Kong</wicri:noRegion></affiliation></author><author><name sortKey="Bojian Zheng" sort="Bojian Zheng" uniqKey="Bojian Zheng" last="Bojian Zheng">BOJIAN ZHENG</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Microbiology, The University of Hong Kong</s1><s3>HKG</s3><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Hong Kong</country><wicri:noRegion>Department of Microbiology, The University of Hong Kong</wicri:noRegion></affiliation></author><author><name sortKey="Jin, Dong Yan" sort="Jin, Dong Yan" uniqKey="Jin D" first="Dong-Yan" last="Jin">Dong-Yan Jin</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Biochemistry, The University of Hong Kong</s1><s3>HKG</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Hong Kong</country><wicri:noRegion>Department of Biochemistry, The University of Hong Kong</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno></seriesStmt></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>Coronavirus</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>Microbiology</term><term>Molecular Chaperones (metabolism)</term><term>Plasmids (metabolism)</term><term>Protein</term><term>Protein Denaturation</term><term>SARS Virus (metabolism)</term><term>Severe acute respiratory syndrome</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term><term>Virology</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="Pascal" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Coronavirus</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>Protéine</term><term>Microbiologie</term><term>Protéines de l'enveloppe virale</term><term>Virologie</term><term>Syndrome respiratoire aigu sévère</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><affiliations><list><country><li>Hong Kong</li></country></list><tree><country name="Hong Kong"><noRegion><name sortKey="Chan, Ching Ping" sort="Chan, Ching Ping" uniqKey="Chan C" first="Ching-Ping" last="Chan">Ching-Ping Chan</name></noRegion><name sortKey="Bojian Zheng" sort="Bojian Zheng" uniqKey="Bojian Zheng" last="Bojian Zheng">BOJIAN ZHENG</name><name sortKey="Chin, King Tung" sort="Chin, King Tung" uniqKey="Chin K" first="King-Tung" last="Chin">King-Tung Chin</name><name sortKey="Jin, Dong Yan" sort="Jin, Dong Yan" uniqKey="Jin D" first="Dong-Yan" last="Jin">Dong-Yan Jin</name><name sortKey="Siu, Kam Leung" sort="Siu, Kam Leung" uniqKey="Siu K" first="Kam-Leung" last="Siu">Kam-Leung Siu</name><name sortKey="Yuen, Kwok Yung" sort="Yuen, Kwok Yung" uniqKey="Yuen K" first="Kwok-Yung" last="Yuen">Kwok-Yung Yuen</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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