Important note: Information in this article was accurate in 1990. The state of the art may have changed since the publication date.
EPSTEIN-BARR VIRUS GLYCOPROTEIN GP85: BIOCHEMICAL CHARACTERISTICS, PURIFICATION AND MAPPING TO VIRAL GENOME
Diss Abstr Int [B]; 50(1):58 1989. Unique Identifier : AIDSLINE ICDB/90658119 Oba DE; Univ. of Florida
Abstract:
Epstein-Barr virus is a human herpesvirus that induces a variety of lymphoproliferative disorders and is implicated in the etiology of two cancers, nasopharyngeal carcinoma and Burkitt's lymphoma. The virus contains at least three glycoproteins in its outer envelope, gp350, gp250, and gp85. When this work began, gp85 had been partially characterized using a monoclonal antibody F.2.1 and shown to contain epitopes that induced neutralizing antibodies; little else was known about the molecule. This dissertation describes additional characterization of gp85 and identification of the gene that encodes it. A new monoclonal antibody, E1D1, was produced and shown to react with gp85. E1D1 was used for purifying gp85 and for preparation of monospecific rabbit antibodies. The BXLF2 open reading frame of the EBV genome, which has homology with the glycoprotein gH of herpes simplex virus, was identified as a candidate gene for gp85. A 17-residue synthetic peptide derived from the BXLF2 sequence was used to raise rabbit antiserum. Anti-peptide antibody was purified from the serum by chromatography on Protein-A agarose and synthetic peptide coupled to Affigel. It was then used to immunoprecipitate a molecule with the same electrophoretic mobility as gp85. Purified anti-peptide antibodies reacted with gp85 in Western blots. Comparison of protease digests of the protein immunoprecipitated by antipeptide antibodies with that recognized by the monoclonal antibody F.2.1 indicated that the two were identical. The polyclonal monospecific rabbit antiserum raised against purified gp85 had a weak, but specific, reaction with the BXLF2 derived peptide in an ELISA. These data indicated that the BXLF2 open reading frame encodes gp85 and thus suggest that gp85 is the EBV equivalent of glycoprotein gH. Two additional synthetic peptides derived from the BXLF2 sequence were used for antibody production in rabbits, and additional monoclonal antibodies to gp85 were produced by a variety of protocols including immunization with whole virus, coupled peptide, or peptide priming followed by challenge with whole virus. These antibodies will be valuable for determining the epitopes of gp85 crucial for neutralization of virus and for study of the functional characteristics of this important surface glycoprotein. (Full text available from University Microfilms International, Ann Arbor, MI, as Order No. AAD89-08265)
Keywords: Antigens, Viral/*GENETICS/ISOLATION & PURIF *Gene Expression Regulation, Viral *Genes, env Herpesvirus 4, Human/*GENETICS Human THESIS 900228
M9020582
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Important note: Information in this article was accurate in 1990. The state of the art may have changed since the publication date.
