Immunological studies on the Epstein-Barr virus encoded alkaline deoxyribonuclease found in virus-producing lymphoblastoid cells

Antisera were raised against a purified recombinant form of the Epstein-Barr virus (EBV) alkaline deoxyri-bonuclease (DNase) expressed in Escherichia coli. These sera were shown to be reactive with lymphoblas-toid cells expressing EBV antigens (B95-8, P3HR-I and Raji). Immunostaining studies of cells expressing EBV antigens revealed that the DNase was a compo-nent of the restricted early antigen complex of EBV. Western blot analysis of these chemically induced cells revealed that the polypeptide associated with the EBV DNase has an Mr of approximately 55000, slightly greater than that of the recombinant form, suggesting that the protein undergoes some form of post-translational modification during virus replication. The DNase enzymic activities observed in B95-8