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

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Abstract
An antibody[Ab]-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 Ig[immunoglobulin]G Ab had anti-EBV activity. It reacted with the membranes and cytoplasm of 7 different EBV-producing lines, but with no non-producing line. The individual cells identified by the murine Ab were the same cells identified by a human serum having anti-EBV activity. Ab significantly reduced the infectivity of 2 independent strains of EBV (P3HR1K and B95-8). The antigen being recognized was characterized by immunoprecipitations of radiolabeled EBV-producer cell lysates. A single glycoprotein with an estimated MW of 250,000 was identified. Neutralization of EBV can be achieved by an IgG-class monoclonal Ab directed against a single antigenic site on a 250,000-dalton glycoprotein, which is a constituent of the EBV virion.