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Antigenic Analysis of the EBV Major Membrane Protein (gp350/gp220) Expressed in Yeast and Mammalian Cells

  • E. A. Emini
  • M. E. Armstrong
  • L. F. Qualtiere
  • G. R. Pearson
  • R. W. Ellis
Part of the Experimental Biology and Medicine book series (EBAM, volume 15)

Abstract

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.

Keywords

Antigenic Determinant Antigenic Analysis Epitope Expression Immune System Recognition Amino Acid Backbone 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© The Humana Press Inc. 1987

Authors and Affiliations

  • E. A. Emini
    • 1
  • M. E. Armstrong
    • 1
  • L. F. Qualtiere
    • 2
  • G. R. Pearson
    • 3
  • R. W. Ellis
    • 1
  1. 1.Merck, Sharp and Dohme Res. Labs.West PointUSA
  2. 2.Univ. of SaskatchewanSaskatoonUSA
  3. 3.School of MedicineGeorgetown Univ.USA

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