Selecting binding and complement-mediated lysis of human hepatoma cells (PLC/PRF/5) in culture by monoclonal antibodies to hepatitis B surface antigen.

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Abstract
High-affinity 125I-labeled monoclonal antibodies to hepatitis B virus surface antigen (HBsAg) bind to a human hepatocellular carcinoma cell line, PLC/PRF/5, which synthesizes and secretes HBsAg. These monoclonal antibodies of the IgG1, IgG2a and IgM isotypes are directed against different antigenic determinants on HBsAg and, in the presence of complement, both anti-HBs IgG2a and IgM, but not anti-HBs IgG1, lyse PLC/PRF/5 cells in culture. Although there is a low level of anti-HBs antibody binding (especially with anti-HBs IgM) to human hepatoma cell lines which do not synthesize HBsAg (SK-Hep 1 and Mahlavu cells), this interaction does not lead to complement-mediated cell lysis and is probably nonspecific. Minimal binding of 125I-labeled anti-influenza hemagglutinin antigen IgM binding to PLC/PRF/5 cells was also detected, but this did not lead to complement-mediated cell lysis. A human hepatocellular carcinoma cell line, persistently infected with hepatitis B virus, can be recognized and lysed by monoclonal antibodies directed against specific determinants of HBsAg. Monoclonal antibodies to this viral envelope protein may prove to be useful immunodiagnostic and immunotherapeutic agents when such viral epitopes are expressed on the surface of infected cells.