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An Epstein-Barr virus (EBV) specific monoclonal antibody (MAb), designated 55H3, was produced after immunizing BALB/c mice with 12-O-tetradecanoylphorbol-13-acetate (TPA) activated B95-8 cells. It was possible to demonstrate that this MAb detected an EBV-specific antigen(s) in the EBV genome-positive producer cell lines B95-8 and M-ABA by immunofluorescence. Immunoglobulin prepared from ascites fluid neutralized the activity of the EBV-encoded DNA polymerase, but not the alkaline DNase. By Western blotting, the 55H3 MAb reacts with an 85/80-KD polypeptide. The 55H3 should be useful in examining the role of EBV DNA polymerase in viral replication.

Partially purified preparations of e-antigen, obtained from sera of hepatitis B antigen carriers, were chromatographed on columns of immobilized single- or double-stranded DNA or on pyran-Sepharose. e-Antigen did not adsorb to any of these columns under conditions appropriate for the retention of various nucleic acid polymerases. Therefore, e-antigen and the DNA polymerase associated with Dane particles can be regarded as distinct proteins.

HSV-2-induced a salt-stimulated DNA polymerase activity in HEp-2 cells at similar levels to that induced by HSV-1 virus at multiplicites of infection from 2 to 20 PFU/cell. De novo synthesis of protein and mRNA was required for DNA polymerase induction by both types. DNA polymerase activity of three strains of each type was compared by response to various salt concentrations and by heat inactivation. Strain-dependent, but not type-dependent differences were found by both tests. Considerable cross-neutralization of polymerase activity was obtained with specific antisera. The DNA polymerase activity induced by HSV-1 and HSV-2 cannot be readily differentiated by these criteria.