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Article: Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein

TitleModulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein
Authors
Issue Date2006
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
Citation
Journal of Virology, 2006, v. 80 n. 18, p. 9279-9287 How to Cite?
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 FKR-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. Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Persistent Identifierhttp://hdl.handle.net/10722/147545
ISSN
2013 Impact Factor: 4.648
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, CPen_HK
dc.contributor.authorSiu, KLen_HK
dc.contributor.authorChin, KTen_HK
dc.contributor.authorYuen, KYen_HK
dc.contributor.authorZheng, Ben_HK
dc.contributor.authorJin, DYen_HK
dc.date.accessioned2012-05-29T06:04:29Z-
dc.date.available2012-05-29T06:04:29Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal of Virology, 2006, v. 80 n. 18, p. 9279-9287en_HK
dc.identifier.issn0022-538Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/147545-
dc.description.abstractPerturbation 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 FKR-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. Copyright © 2006, American Society for Microbiology. All Rights Reserved.en_HK
dc.languageengen_US
dc.publisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/en_HK
dc.relation.ispartofJournal of Virologyen_HK
dc.subject.meshAnimalsen_US
dc.subject.meshCcaat-Enhancer-Binding Proteins - Metabolismen_US
dc.subject.meshCell Lineen_US
dc.subject.meshCercopithecus Aethiopsen_US
dc.subject.meshEndoplasmic Reticulum - Metabolismen_US
dc.subject.meshHsp70 Heat-Shock Proteins - Metabolismen_US
dc.subject.meshHeat-Shock Proteins - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshMembrane Glycoproteins - Chemistryen_US
dc.subject.meshMembrane Proteins - Metabolismen_US
dc.subject.meshMolecular Chaperones - Metabolismen_US
dc.subject.meshPlasmids - Metabolismen_US
dc.subject.meshProtein Denaturationen_US
dc.subject.meshSars Virus - Metabolismen_US
dc.subject.meshVero Cellsen_US
dc.subject.meshViral Envelope Proteins - Chemistryen_US
dc.titleModulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike proteinen_HK
dc.typeArticleen_HK
dc.identifier.emailYuen, KY:kyyuen@hkucc.hku.hken_HK
dc.identifier.emailZheng, B:bzheng@hkucc.hku.hken_HK
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_HK
dc.identifier.authorityYuen, KY=rp00366en_HK
dc.identifier.authorityZheng, B=rp00353en_HK
dc.identifier.authorityJin, DY=rp00452en_HK
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1128/JVI.00659-06en_HK
dc.identifier.pmid16940539en_HK
dc.identifier.scopuseid_2-s2.0-33748502744en_HK
dc.identifier.hkuros119561-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33748502744&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume80en_HK
dc.identifier.issue18en_HK
dc.identifier.spage9279en_HK
dc.identifier.epage9287en_HK
dc.identifier.isiWOS:000240384800043-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChan, CP=7404813842en_HK
dc.identifier.scopusauthoridSiu, KL=7102312040en_HK
dc.identifier.scopusauthoridChin, KT=7202995491en_HK
dc.identifier.scopusauthoridYuen, KY=36078079100en_HK
dc.identifier.scopusauthoridZheng, B=7201780588en_HK
dc.identifier.scopusauthoridJin, DY=7201973614en_HK

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