Polypeptides of the Epstein-Barr virus membrane antigen complex

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Abstract
Epstein-Barr virus (EBV)-associated membrane antigens were purified from the plasma membranes of the producer [human Burkitts'' lymphoma] cell line P3HR-1 NONO. The antigens were assayed with a specific rabbit anti-EBV antiserum using an 125I-labeled staphyloccocal protein A binding assay. The antigens were present on purified plasma membranes. Treatment of the plasma membranes with Triton X-100 allows the separation of 2 antigenically distinct classes of antigens, 1 soluble and 1 insoluble in the detergent. Immunoprecipitates of [125I]- and [35S]methionine-labeled, detergent-soluble antigens contained 3 major polypeptides of MW 350,000, 140,000 and 75,000 (on 7.5% sodium dodecyl sulfate-polyacrylamide gel electrophoresis) and several minor components. These polypeptides were all specifically precipitated from 4 EBV-producer cell lines, P3HR-1, P3HR-1 NONO, B95-8 and 7744. They could not be precipitated from producer cell lines treated with phosphonoacetic acid, which inhibits late viral functions, nor could they be precipitated from nonproducer cell lines. The 350,000 and 75,000 MW polypeptides bound to ricin and lentil lectin columns, but most of the 140,000 MW material did not. A component of MW 220,000 (prominent only in P3HR-1 NONO) was probably a degradation product of the 350,000 MW polypeptide.