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dc.contributor.authorStewart, J P
dc.contributor.authorJanjua, N J
dc.contributor.authorPepper, Stuart D
dc.contributor.authorBennion, Gordon
dc.contributor.authorMackett, Mike
dc.contributor.authorAllen, Terence D
dc.contributor.authorNash, A A
dc.contributor.authorArrand, John R
dc.date.accessioned2010-04-07T14:41:53Z
dc.date.available2010-04-07T14:41:53Z
dc.date.issued1996-06
dc.identifier.citationIdentification and characterization of murine gammaherpesvirus 68 gp150: a virion membrane glycoprotein. 1996, 70 (6):3528-35 J. Virol.en
dc.identifier.issn0022-538X
dc.identifier.pmid8648686
dc.identifier.urihttp://hdl.handle.net/10541/95892
dc.description.abstractMurine gammaherpesvirus 68 (MHV-68) is a naturally occurring virus of murid rodents which displays pathobiological characteristics similar to those of other gammaherpesviruses, including Epstein-Barr virus (EBV). However, unlike EBV and many other gammaherpesviruses, MHV-68 replicates in epithelial cells in vitro and infects laboratory strains of mice and therefore provides a good model for the study of gammaherpesviruses. Studies of sequences around the center of the MHV-68 genome identified a gene (designated BPRF1 for BamHI P fragment rightward open reading frame 1) whose putative product had motifs reminiscent of a transmembrane glycoprotein. All other gammaherpesviruses have a glycoprotein in this genomic position, but the BPRF1 gene showed sequence homology with only the EBV membrane antigen gp340/220. Biochemical analysis showed that the product of BPRF1 was a glycoprotein present on the surface of infected cells, and immunoelectron microscopy showed that it was present in the virus particle. In addition, antibodies to the BPRF1 product raised by using a bacterial fusion protein neutralized the virus in the absence of complement. The predominant molecular weights of the protein were 150,000 and 130,000. Pulse-chase analysis and endoglycosidase-H digestion showed that the 130,000-molecular-weight form was a precursor of the 150,000-molecular-weight form, and cell surface labelling showed that the 150,000-molecular-weight form alone was on the cell surface. We therefore named the protein gp150. Since gp150 is the first virion-associated glycoprotein and neutralizing determinant of MHV-68 to be characterized, it provides a valuable tool for the future study of virus-host interactions.
dc.language.isoenen
dc.subject.meshAmino Acid Sequence
dc.subject.meshAnimals
dc.subject.meshBase Sequence
dc.subject.meshGammaherpesvirinae
dc.subject.meshGenes, Viral
dc.subject.meshMembrane Glycoproteins
dc.subject.meshMice
dc.subject.meshMolecular Sequence Data
dc.subject.meshMolecular Weight
dc.subject.meshViral Envelope Proteins
dc.subject.meshVirion
dc.titleIdentification and characterization of murine gammaherpesvirus 68 gp150: a virion membrane glycoprotein.en
dc.typeArticleen
dc.contributor.departmentDepartment of Veterinary Pathology, The University of Edinburgh, United Kingdom.en
dc.identifier.journalJournal of Virologyen
html.description.abstractMurine gammaherpesvirus 68 (MHV-68) is a naturally occurring virus of murid rodents which displays pathobiological characteristics similar to those of other gammaherpesviruses, including Epstein-Barr virus (EBV). However, unlike EBV and many other gammaherpesviruses, MHV-68 replicates in epithelial cells in vitro and infects laboratory strains of mice and therefore provides a good model for the study of gammaherpesviruses. Studies of sequences around the center of the MHV-68 genome identified a gene (designated BPRF1 for BamHI P fragment rightward open reading frame 1) whose putative product had motifs reminiscent of a transmembrane glycoprotein. All other gammaherpesviruses have a glycoprotein in this genomic position, but the BPRF1 gene showed sequence homology with only the EBV membrane antigen gp340/220. Biochemical analysis showed that the product of BPRF1 was a glycoprotein present on the surface of infected cells, and immunoelectron microscopy showed that it was present in the virus particle. In addition, antibodies to the BPRF1 product raised by using a bacterial fusion protein neutralized the virus in the absence of complement. The predominant molecular weights of the protein were 150,000 and 130,000. Pulse-chase analysis and endoglycosidase-H digestion showed that the 130,000-molecular-weight form was a precursor of the 150,000-molecular-weight form, and cell surface labelling showed that the 150,000-molecular-weight form alone was on the cell surface. We therefore named the protein gp150. Since gp150 is the first virion-associated glycoprotein and neutralizing determinant of MHV-68 to be characterized, it provides a valuable tool for the future study of virus-host interactions.


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