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Conference Paper: Severe acute respiratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus release

TitleSevere acute respiratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus release
Authors
Issue Date2006
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings of the National Academy of Sciences of the United States of America, 2006, v. 103 n. 33, p. 12540-12545 How to Cite?
AbstractFourteen ORFs have been identified in the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) genome. ORF 3a of SARS-CoV codes for a recently identified transmembrane protein, but its function remains unknown. In this study we confirmed the 3a protein expression and investigated its localization at the surface of SARS-CoV-infected or 3a-cDNA-transfected cells. Our experiments showed that recombinant 3a protein can form a homotetramer complex through interprotein disulfide bridges in 3a-cDNA-transfected cells, providing a clue to ion channel function. The putative ion channel activity of this protein was assessed in 3a-complement RNA-injected Xenopus oocytes by two-electrode voltage clamp. The results suggest that 3a protein forms a potassium sensitive channel, which can be efficiently inhibited by barium. After FRhK-4 cells were transfected with an siRNA, which is known to suppress 3a expression, followed by infection with SARS-CoV, the released virus was significantly decreased, whereas the replication of the virus in the infected cells was not changed. Our observation suggests that SARS-CoV ORF 3a functions as an ion channel that may promote virus release. This finding will help to explain the highly pathogenic nature of SARS-CoV and to develop new strategies for treatment of SARS infection. © 2006 by The National Academy of Sciences of the USA.
Persistent Identifierhttp://hdl.handle.net/10722/157455
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLu, Wen_US
dc.contributor.authorZheng, Ben_US
dc.contributor.authorXu, Ken_US
dc.contributor.authorSchwarz, Wen_US
dc.contributor.authorDu, Len_US
dc.contributor.authorWong, CKLen_US
dc.contributor.authorChen, Jen_US
dc.contributor.authorDuan, Sen_US
dc.contributor.authorDeubel, Ven_US
dc.contributor.authorSun, Ben_US
dc.date.accessioned2012-08-08T08:50:06Z-
dc.date.available2012-08-08T08:50:06Z-
dc.date.issued2006en_US
dc.identifier.citationProceedings of the National Academy of Sciences of the United States of America, 2006, v. 103 n. 33, p. 12540-12545en_US
dc.identifier.issn0027-8424en_US
dc.identifier.urihttp://hdl.handle.net/10722/157455-
dc.description.abstractFourteen ORFs have been identified in the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) genome. ORF 3a of SARS-CoV codes for a recently identified transmembrane protein, but its function remains unknown. In this study we confirmed the 3a protein expression and investigated its localization at the surface of SARS-CoV-infected or 3a-cDNA-transfected cells. Our experiments showed that recombinant 3a protein can form a homotetramer complex through interprotein disulfide bridges in 3a-cDNA-transfected cells, providing a clue to ion channel function. The putative ion channel activity of this protein was assessed in 3a-complement RNA-injected Xenopus oocytes by two-electrode voltage clamp. The results suggest that 3a protein forms a potassium sensitive channel, which can be efficiently inhibited by barium. After FRhK-4 cells were transfected with an siRNA, which is known to suppress 3a expression, followed by infection with SARS-CoV, the released virus was significantly decreased, whereas the replication of the virus in the infected cells was not changed. Our observation suggests that SARS-CoV ORF 3a functions as an ion channel that may promote virus release. This finding will help to explain the highly pathogenic nature of SARS-CoV and to develop new strategies for treatment of SARS infection. © 2006 by The National Academy of Sciences of the USA.en_US
dc.languageengen_US
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.orgen_US
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americaen_US
dc.rightsProceedings of the National Academy of Sciences. Copyright © National Academy of Sciences.-
dc.subject.meshAnimalsen_US
dc.subject.meshCell Lineen_US
dc.subject.meshHumansen_US
dc.subject.meshIon Channels - Genetics - Metabolismen_US
dc.subject.meshOocytes - Cytology - Physiologyen_US
dc.subject.meshOpen Reading Framesen_US
dc.subject.meshPatch-Clamp Techniquesen_US
dc.subject.meshPotassium - Metabolismen_US
dc.subject.meshRna, Small Interfering - Genetics - Metabolismen_US
dc.subject.meshRecombinant Proteins - Genetics - Metabolismen_US
dc.subject.meshSars Virus - Genetics - Metabolismen_US
dc.subject.meshViral Proteins - Genetics - Metabolismen_US
dc.subject.meshVirus Replicationen_US
dc.subject.meshXenopus Laevisen_US
dc.titleSevere acute respiratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus releaseen_US
dc.typeConference_Paperen_US
dc.identifier.emailZheng, B: bzheng@hkucc.hku.hken_US
dc.identifier.authorityZheng, BJ=rp00353en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1073/pnas.0605402103en_US
dc.identifier.pmid16894145-
dc.identifier.scopuseid_2-s2.0-33747617366en_US
dc.identifier.hkuros132255-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33747617366&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume103en_US
dc.identifier.issue33en_US
dc.identifier.spage12540en_US
dc.identifier.epage12545en_US
dc.identifier.isiWOS:000239867500061-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLu, W=36077781100en_US
dc.identifier.scopusauthoridZheng, BJ=7201780588en_US
dc.identifier.scopusauthoridXu, K=7403282210en_US
dc.identifier.scopusauthoridSchwarz, W=7202953793en_US
dc.identifier.scopusauthoridDu, L=8686996200en_US
dc.identifier.scopusauthoridWong, CKL=36862848200en_US
dc.identifier.scopusauthoridChen, J=14119348200en_US
dc.identifier.scopusauthoridDuan, S=36865040200en_US
dc.identifier.scopusauthoridDeubel, V=7005679225en_US
dc.identifier.scopusauthoridSun, B=24734369900en_US
dc.customcontrol.immutablesml 161207 - amended-

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