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Article: Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein
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TitleModulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein
 
AuthorsChan, CP1
Siu, KL1
Chin, KT1
Yuen, KY1
Zheng, B1
Jin, DY1
 
Issue Date2006
 
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
 
CitationJournal of Virology, 2006, v. 80 n. 18, p. 9279-9287 [How to Cite?]
DOI: http://dx.doi.org/10.1128/JVI.00659-06
 
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.
 
ISSN0022-538X
2012 Impact Factor: 5.076
2012 SCImago Journal Rankings: 2.559
 
DOIhttp://dx.doi.org/10.1128/JVI.00659-06
 
ISI Accession Number IDWOS:000240384800043
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorChan, CP
 
dc.contributor.authorSiu, KL
 
dc.contributor.authorChin, KT
 
dc.contributor.authorYuen, KY
 
dc.contributor.authorZheng, B
 
dc.contributor.authorJin, DY
 
dc.date.accessioned2012-05-29T06:04:29Z
 
dc.date.available2012-05-29T06:04:29Z
 
dc.date.issued2006
 
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.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationJournal of Virology, 2006, v. 80 n. 18, p. 9279-9287 [How to Cite?]
DOI: http://dx.doi.org/10.1128/JVI.00659-06
 
dc.identifier.doihttp://dx.doi.org/10.1128/JVI.00659-06
 
dc.identifier.epage9287
 
dc.identifier.hkuros119561
 
dc.identifier.isiWOS:000240384800043
 
dc.identifier.issn0022-538X
2012 Impact Factor: 5.076
2012 SCImago Journal Rankings: 2.559
 
dc.identifier.issue18
 
dc.identifier.pmid16940539
 
dc.identifier.scopuseid_2-s2.0-33748502744
 
dc.identifier.spage9279
 
dc.identifier.urihttp://hdl.handle.net/10722/147545
 
dc.identifier.volume80
 
dc.languageeng
 
dc.publisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
 
dc.publisher.placeUnited States
 
dc.relation.ispartofJournal of Virology
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAnimals
 
dc.subject.meshCcaat-Enhancer-Binding Proteins - Metabolism
 
dc.subject.meshCell Line
 
dc.subject.meshCercopithecus Aethiops
 
dc.subject.meshEndoplasmic Reticulum - Metabolism
 
dc.subject.meshHsp70 Heat-Shock Proteins - Metabolism
 
dc.subject.meshHeat-Shock Proteins - Metabolism
 
dc.subject.meshHumans
 
dc.subject.meshMembrane Glycoproteins - Chemistry
 
dc.subject.meshMembrane Proteins - Metabolism
 
dc.subject.meshMolecular Chaperones - Metabolism
 
dc.subject.meshPlasmids - Metabolism
 
dc.subject.meshProtein Denaturation
 
dc.subject.meshSars Virus - Metabolism
 
dc.subject.meshVero Cells
 
dc.subject.meshViral Envelope Proteins - Chemistry
 
dc.titleModulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong