Monoclonal antibodies against the major glycoprotein (gp350/220) of Epstein-Barr virus neutralize infectivity.

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Abstract
Hybridomas [derived from murine myeloma NS-1 and spleen cells] producing antibodies against Epstein-Barr virus (EBV) were produced. They were screened for production of antibodies against the EBV-associated membrane antigens on EBV producer cell lines. A double-antibody radioimmunoassay with 125I-labeled rabbit anti-mouse Ig was used. Positive cultures were cloned and 1 such clone, C1, was used for further study. C1 antibody neutralizes EBV in vitro and immunoprecipitates gp350 (the major glycoprotein in B95-8 [marmoset neoplastic leukocyte] cells) and gp220 (the major glycoprotein in P3HR-1 [human lymphoma] cells) from the membrane antigen complex, suggesting that these molecules are antigenically related. The presence of gp350/220 both on the plasma membrane and in the cytoplasm may be detected by immunofluorescence with C1 antibody.