File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: BiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion component

TitleBiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion component
Authors
Issue Date1998
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
Citation
Journal Of Virology, 1998, v. 72 n. 12, p. 9865-9872 How to Cite?
AbstractRotavirus infection induces profound alterations in the morphology and biochemistry of the host cell. Using two-dimensional (2D) gel electrophoresis combined with metabolic labeling, we have identified four proteins that are specifically upregulated in rotavirus-infected cells. Two of these have been identified as BiP (GRP78) and endoplasmin (GRP94), members of a family of glucose-regulated chaperone proteins that reside in the endoplasmic reticulum (ER) lumen, the site of rotavirus morphogenesis. The level of mRNA nd the transcriptional activity of the BiP and endoplasmin genes are increased markedly in rotavirus-infected cells, and these genes are also induced when a single rotavirus protein, the nonstructural glycoprotein NSP4, is expressed in MA104 cells. However, NSP4 does not associate with either BiP or endoplasmin, implying that the mechanism of BiP and endoplasmin gene activation by NSP4 may differ from that triggered by viral membrane glycoproteins of other viruses. The interaction of BiP and endoplasmin with rotavirus structural polypeptides suggests that these chaperones are involved in the process of viral maturation in the ER lumen.
Persistent Identifierhttp://hdl.handle.net/10722/162232
ISSN
2023 Impact Factor: 4.0
2023 SCImago Journal Rankings: 1.378
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXu, Aen_US
dc.contributor.authorBellamy, ARen_US
dc.contributor.authorTaylor, JAen_US
dc.date.accessioned2012-09-05T05:18:17Z-
dc.date.available2012-09-05T05:18:17Z-
dc.date.issued1998en_US
dc.identifier.citationJournal Of Virology, 1998, v. 72 n. 12, p. 9865-9872en_US
dc.identifier.issn0022-538Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/162232-
dc.description.abstractRotavirus infection induces profound alterations in the morphology and biochemistry of the host cell. Using two-dimensional (2D) gel electrophoresis combined with metabolic labeling, we have identified four proteins that are specifically upregulated in rotavirus-infected cells. Two of these have been identified as BiP (GRP78) and endoplasmin (GRP94), members of a family of glucose-regulated chaperone proteins that reside in the endoplasmic reticulum (ER) lumen, the site of rotavirus morphogenesis. The level of mRNA nd the transcriptional activity of the BiP and endoplasmin genes are increased markedly in rotavirus-infected cells, and these genes are also induced when a single rotavirus protein, the nonstructural glycoprotein NSP4, is expressed in MA104 cells. However, NSP4 does not associate with either BiP or endoplasmin, implying that the mechanism of BiP and endoplasmin gene activation by NSP4 may differ from that triggered by viral membrane glycoproteins of other viruses. The interaction of BiP and endoplasmin with rotavirus structural polypeptides suggests that these chaperones are involved in the process of viral maturation in the ER lumen.en_US
dc.languageengen_US
dc.publisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/en_US
dc.relation.ispartofJournal of Virologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCarrier Proteins - Biosynthesis - Genetics - Metabolismen_US
dc.subject.meshCell Lineen_US
dc.subject.meshEndoplasmic Reticulum - Metabolism - Virologyen_US
dc.subject.meshGene Expressionen_US
dc.subject.meshGlycoproteins - Geneticsen_US
dc.subject.meshHsp70 Heat-Shock Proteins - Biosynthesis - Genetics - Metabolismen_US
dc.subject.meshHeat-Shock Proteinsen_US
dc.subject.meshMacaca Mulattaen_US
dc.subject.meshMembrane Proteins - Biosynthesis - Genetics - Metabolismen_US
dc.subject.meshMolecular Chaperones - Biosynthesis - Genetics - Metabolismen_US
dc.subject.meshRna, Messenger - Genetics - Metabolismen_US
dc.subject.meshRotavirus - Genetics - Growth & Development - Pathogenicityen_US
dc.subject.meshRotavirus Infections - Genetics - Metabolism - Virologyen_US
dc.subject.meshToxins, Biologicalen_US
dc.subject.meshViral Nonstructural Proteins - Geneticsen_US
dc.titleBiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion componenten_US
dc.typeArticleen_US
dc.identifier.emailXu, A:amxu@hkucc.hku.hken_US
dc.identifier.authorityXu, A=rp00485en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1128/JVI.72.12.9865-9872.1998-
dc.identifier.pmid9811722-
dc.identifier.scopuseid_2-s2.0-0031797727en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031797727&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume72en_US
dc.identifier.issue12en_US
dc.identifier.spage9865en_US
dc.identifier.epage9872en_US
dc.identifier.isiWOS:000076892100049-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridXu, A=7202655409en_US
dc.identifier.scopusauthoridBellamy, AR=7004515654en_US
dc.identifier.scopusauthoridTaylor, JA=24781484000en_US
dc.identifier.issnl0022-538X-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats