Antigenic Analysis of the EBV Major Membrane Protein (gp350/gp220) Expressed in Yeast and Mammalian Cells
The Epstein-Barr virus (EBV) major membrane protein (gp350/gp220) has been identified as the primary mediator of virus-cell receptor interaction (1) and as an inducer of in vitro virus-neutralizing antibody (2,3,4). Under certain circumstances, the purified membrane protein has been shown to confer protection in model primate animals against the effects of EBV infection (5). The protein is highly glycosylated. Fifty percent of its molecular mass is due to carbohydrate. The identification of the gene which codes for gp350/gp220 has allowed for the expression of the protein in bacteria (6), yeast and mammalian cells. Table 1 lists the systems in which expression has been obtained and the structural characteristics of the expressed proteins. See the accompanying papers of this volume for details. In this report, we describe the results of our antigenic analyses of these proteins as well as of the membrane antigen derived from the B95–8 EBV-transformed marmoset lymphoid cell line. The analyses were designed to determine the immunogenic feasibility of each of the antigens as sub-unit vaccine candidates.
KeywordsCarbohydrate Saccharomyces Sera
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