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
2011 Impact Factor: 5.402
2011 SCImago Journal Rankings: 0.745
DOIhttp://dx.doi.org/10.1128/JVI.00659-06
ISI Accession Number IDWOS:000240384800043
ReferencesReferences in Scopus
DC Field
Value
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
2011 Impact Factor: 5.402
2011 SCImago Journal Rankings: 0.745
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
Author Affiliations
  1. The University of Hong Kong