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Characterization and expression of a glycoprotein encoded by the Epstein-Barr virus BamHI I fragment.

dc.contributor.authorMackett, Mike
dc.contributor.authorConway, Margaret J
dc.contributor.authorArrand, John R
dc.contributor.authorHaddad, R S
dc.contributor.authorHutt-Fletcher, L M
dc.date.accessioned2010-08-18T08:21:30Z
dc.date.available2010-08-18T08:21:30Z
dc.date.issued1990-06
dc.identifier.citationCharacterization and expression of a glycoprotein encoded by the Epstein-Barr virus BamHI I fragment. 1990, 64 (6):2545-52 J. Virol.en
dc.identifier.issn0022-538X
dc.identifier.pmid2159529
dc.identifier.urihttp://hdl.handle.net/10541/109794
dc.description.abstractComputer-assisted analysis of the Epstein-Barr virus (EBV) open reading frame BILF2 (B95-8 nucleotides 150,525 to 149,782) predicts that it codes for a membrane-bound glycoprotein. [3H]glucosamine labeling of cells infected with vaccinia virus recombinants that expressed the BILF2 open reading frame revealed several diffuse species of glycoproteins of around 80,000 and 55,000 daltons. A monoclonal antibody derived from spleens of mice immunized with EBV immunoprecipitated the EBV-derived protein made by the vaccinia virus recombinants and also precipitated a late envelope glycoprotein with a mobility of 78,000 to 55,000 from EBV-producing cells. N-Glycanase treatment of the immunoprecipitated BILF2 product from EBV-producing cells resulted in a polypeptide of 28 kilodaltons, closely agreeing with the predicted molecular mass for the unmodified BILF2 gene product. Western (immuno-) blots using recombinant infected cells as a source of antigen showed that the majority of EBV-seropositive individuals have a serum antibody response to the BILF2-encoded gp78/55.
dc.language.isoenen
dc.subject.meshAmino Acid Sequence
dc.subject.meshAntibodies, Monoclonal
dc.subject.meshBase Sequence
dc.subject.meshBlotting, Western
dc.subject.meshCell Line
dc.subject.meshDeoxyribonuclease BamHI
dc.subject.meshFluorescent Antibody Technique
dc.subject.meshGenes, Viral
dc.subject.meshGlycoproteins
dc.subject.meshHerpesvirus 4, Human
dc.subject.meshHumans
dc.subject.meshImmunoglobulin G
dc.subject.meshMolecular Sequence Data
dc.subject.meshPlasmids
dc.subject.meshRestriction Mapping
dc.subject.meshVaccinia virus
dc.subject.meshViral Proteins
dc.titleCharacterization and expression of a glycoprotein encoded by the Epstein-Barr virus BamHI I fragment.en
dc.typeArticleen
dc.contributor.departmentCancer Research Campaign Laboratories, Paterson Institute for Cancer Research, Christie Hospital and Holt Radium Institute, Manchester, United Kingdom.en
dc.identifier.journalJournal of Virologyen
html.description.abstractComputer-assisted analysis of the Epstein-Barr virus (EBV) open reading frame BILF2 (B95-8 nucleotides 150,525 to 149,782) predicts that it codes for a membrane-bound glycoprotein. [3H]glucosamine labeling of cells infected with vaccinia virus recombinants that expressed the BILF2 open reading frame revealed several diffuse species of glycoproteins of around 80,000 and 55,000 daltons. A monoclonal antibody derived from spleens of mice immunized with EBV immunoprecipitated the EBV-derived protein made by the vaccinia virus recombinants and also precipitated a late envelope glycoprotein with a mobility of 78,000 to 55,000 from EBV-producing cells. N-Glycanase treatment of the immunoprecipitated BILF2 product from EBV-producing cells resulted in a polypeptide of 28 kilodaltons, closely agreeing with the predicted molecular mass for the unmodified BILF2 gene product. Western (immuno-) blots using recombinant infected cells as a source of antigen showed that the majority of EBV-seropositive individuals have a serum antibody response to the BILF2-encoded gp78/55.


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