Identification and characterization of murine gammaherpesvirus 68 gp150: a virion membrane glycoprotein.

2.50
Hdl Handle:
http://hdl.handle.net/10541/95892
Title:
Identification and characterization of murine gammaherpesvirus 68 gp150: a virion membrane glycoprotein.
Authors:
Stewart, J P; Janjua, N J; Pepper, Stuart D; Bennion, Gordon; Mackett, Mike; Allen, Terence D; Nash, A A; Arrand, John R
Abstract:
Murine 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.
Affiliation:
Department of Veterinary Pathology, The University of Edinburgh, United Kingdom.
Citation:
Identification and characterization of murine gammaherpesvirus 68 gp150: a virion membrane glycoprotein. 1996, 70 (6):3528-35 J. Virol.
Journal:
Journal of Virology
Issue Date:
Jun-1996
URI:
http://hdl.handle.net/10541/95892
PubMed ID:
8648686
Type:
Article
Language:
en
ISSN:
0022-538X
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorStewart, J Pen
dc.contributor.authorJanjua, N Jen
dc.contributor.authorPepper, Stuart Den
dc.contributor.authorBennion, Gordonen
dc.contributor.authorMackett, Mikeen
dc.contributor.authorAllen, Terence Den
dc.contributor.authorNash, A Aen
dc.contributor.authorArrand, John Ren
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.en
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

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