Monoclonal antibody against a 250,000-dalton glycoprotein of Epstein-Barr virus identifies a membrane antigen and a neutralizing antigen

G. J. Hoffman, S. G. Lazarowitz, S. D. Hayward

Research output: Contribution to journalArticle

Abstract

An antibody-secreting hybrid cell line was produced by fusion of mouse myeloma cells with splenocytes from mice immunized with virions of the B95-8 strain of Epstein-Barr Virus (EBV). The monoclonal IgG antibody was shown to have anti-EBV activity by the following criteria: It reacted with the membranes and the cytoplasm of seven different EBV-producing lines, but with no nonproducing line. The individual cells identified by the murine antibody were shown to be the same cells identified by a human serum having anti-EBV activity. The antibody significantly reduced the infectivity of two independent strains of EBV (namely, P3HR1K and B95-8). The antigen being recognized was characterized by immunoprecipitations of radiolabeled EBV-producer cell lysates. A single glycoprotein with an estimated molecular weight of 250,000 was identified. It is concluded that neutralization of EBV can be achieved by an IgG-class monoclonal antibody directed against a single antigenic site on a 250,000-dalton glycoprotein, which is a constituent of the EBV virion.

Original languageEnglish (US)
Pages (from-to)2979-2983
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume77
Issue number5 I
DOIs
StatePublished - Jan 1 1980

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