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Article: Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E

TitleDifferential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E
Authors
Issue Date2005
PublisherSociety for General Microbiology. The Journal's web site is located at http://vir.sgmjournals.org
Citation
Journal Of General Virology, 2005, v. 86 n. 5, p. 1423-1434 How to Cite?
AbstractPost-translational modifications and correct subcellular localization of viral structural proteins are prerequisites for assembly and budding of enveloped viruses. Coronaviruses, like the severe acute respiratory syndrome-associated virus (SARS-CoV), bud from the endoplasmic reticulum-Golgi intermediate compartment. In this study, the subcellular distribution and maturation of SARS-CoV surface proteins S, M and E were analysed by using C-terminally tagged proteins. As early as 30 min post-entry into the endoplasmic reticulum, high-mannosylated S assembles into trimers prior to acquisition of complex N-glycans in the Golgi. Like S, M acquires high-mannose N-glycans that are subsequently modified into complex N-glycans in the Golgi. The N-glycosylation profile and the absence of O-glycosylation on M protein relate SARS-CoV to the previously described group 1 and 3 coronaviruses. Immunofluorescence analysis shows that S is detected in several compartments along the secretory pathway from the endoplasmic reticulum to the plasma membrane while M predominantly localizes in the Golgi, where it accumulates, and in trafficking vesicles. The E protein is not glycosylated. Pulse-chase labelling and confocal microscopy in the presence of protein translation inhibitor cycloheximide revealed that the E protein has a short half-life of 30 min. E protein is found in bright perinuclear patches colocalizing with endoplasmic reticulum markers. In conclusion, SARS-CoV surface proteins S, M and E show differential subcellular localizations when expressed alone suggesting that additional cellular or viral factors might be required for coordinated trafficking to the virus assembly site in the endoplasmic reticulum-Golgi intermediate compartment. © 2005 SGM.
Persistent Identifierhttp://hdl.handle.net/10722/48635
ISSN
2015 Impact Factor: 3.192
2015 SCImago Journal Rankings: 1.741
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorNal, Ben_HK
dc.contributor.authorChan, Cen_HK
dc.contributor.authorKien, Fen_HK
dc.contributor.authorSiu, Len_HK
dc.contributor.authorTse, Jen_HK
dc.contributor.authorChu, Ken_HK
dc.contributor.authorKam, Jen_HK
dc.contributor.authorStaropoli, Ien_HK
dc.contributor.authorCrescenzoChaigne, Ben_HK
dc.contributor.authorEscriou, Nen_HK
dc.contributor.authorvan der Wef, Sen_HK
dc.contributor.authorYuen, KYen_HK
dc.contributor.authorAltmeyer, Ren_HK
dc.date.accessioned2008-05-22T04:19:39Z-
dc.date.available2008-05-22T04:19:39Z-
dc.date.issued2005en_HK
dc.identifier.citationJournal Of General Virology, 2005, v. 86 n. 5, p. 1423-1434en_HK
dc.identifier.issn0022-1317en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48635-
dc.description.abstractPost-translational modifications and correct subcellular localization of viral structural proteins are prerequisites for assembly and budding of enveloped viruses. Coronaviruses, like the severe acute respiratory syndrome-associated virus (SARS-CoV), bud from the endoplasmic reticulum-Golgi intermediate compartment. In this study, the subcellular distribution and maturation of SARS-CoV surface proteins S, M and E were analysed by using C-terminally tagged proteins. As early as 30 min post-entry into the endoplasmic reticulum, high-mannosylated S assembles into trimers prior to acquisition of complex N-glycans in the Golgi. Like S, M acquires high-mannose N-glycans that are subsequently modified into complex N-glycans in the Golgi. The N-glycosylation profile and the absence of O-glycosylation on M protein relate SARS-CoV to the previously described group 1 and 3 coronaviruses. Immunofluorescence analysis shows that S is detected in several compartments along the secretory pathway from the endoplasmic reticulum to the plasma membrane while M predominantly localizes in the Golgi, where it accumulates, and in trafficking vesicles. The E protein is not glycosylated. Pulse-chase labelling and confocal microscopy in the presence of protein translation inhibitor cycloheximide revealed that the E protein has a short half-life of 30 min. E protein is found in bright perinuclear patches colocalizing with endoplasmic reticulum markers. In conclusion, SARS-CoV surface proteins S, M and E show differential subcellular localizations when expressed alone suggesting that additional cellular or viral factors might be required for coordinated trafficking to the virus assembly site in the endoplasmic reticulum-Golgi intermediate compartment. © 2005 SGM.en_HK
dc.format.extent663037 bytes-
dc.format.extent159135 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypeapplication/pdf-
dc.languageengen_HK
dc.publisherSociety for General Microbiology. The Journal's web site is located at http://vir.sgmjournals.orgen_HK
dc.relation.ispartofJournal of General Virologyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshProtein Processing, Post-Translationalen_HK
dc.subject.meshProtein Transporten_HK
dc.subject.meshSARS Virus - growth & developmenten_HK
dc.subject.meshMembrane Glycoproteins - analysis - chemistry - metabolismen_HK
dc.subject.meshViral Envelope Proteins - analysis - chemistry - metabolismen_HK
dc.titleDifferential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and Een_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-1317&volume=86&issue=pt 5&spage=1423&epage=1434&date=2005&atitle=Differential+maturation+and+subcellular+localization+of+severe+acute+respiratory+syndrome+coronavirus+surface+proteins+S,+M+and+Een_HK
dc.identifier.emailNal, B: bnal@hkucc.hku.hken_HK
dc.identifier.emailYuen, KY: kyyuen@hkucc.hku.hken_HK
dc.identifier.authorityNal, B=rp00541en_HK
dc.identifier.authorityYuen, KY=rp00366en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1099/vir.0.80671-0en_HK
dc.identifier.pmid15831954-
dc.identifier.scopuseid_2-s2.0-20944432579en_HK
dc.identifier.hkuros100503-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-20944432579&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume86en_HK
dc.identifier.issue5en_HK
dc.identifier.spage1423en_HK
dc.identifier.epage1434en_HK
dc.identifier.isiWOS:000228717200021-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridNal, B=6506672380en_HK
dc.identifier.scopusauthoridChan, C=7404814453en_HK
dc.identifier.scopusauthoridKien, F=7004231633en_HK
dc.identifier.scopusauthoridSiu, L=7006651164en_HK
dc.identifier.scopusauthoridTse, J=36928243100en_HK
dc.identifier.scopusauthoridChu, K=8415242400en_HK
dc.identifier.scopusauthoridKam, J=8415242500en_HK
dc.identifier.scopusauthoridStaropoli, I=8415242600en_HK
dc.identifier.scopusauthoridCrescenzoChaigne, B=6603401918en_HK
dc.identifier.scopusauthoridEscriou, N=6603606703en_HK
dc.identifier.scopusauthoridvan der Wef, S=8415242900en_HK
dc.identifier.scopusauthoridYuen, KY=36078079100en_HK
dc.identifier.scopusauthoridAltmeyer, R=7003677186en_HK

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