CHARACTERIZATION OF MONOCLONAL-ANTIBODIES TO THE ZTA AND DNASE PROTEINS OF EPSTEIN-BARR-VIRUS

Two monoclonal antibodies (mAb) were derived and designated 4F10 and 3 11H. 4F10 was against the Epstein-Barr virus (EBV) Zta protein and 311 H specifically recognized EBV DNase enzyme. Using mAb 4F10 as a probe , the Zta protein could be detected as a 36-kD molecule in L5 cells an d as a 38-kD molecule in B95-8 cells, reflecting the fact reported by other laboratories, using rabbit polyclonal antisera, that the Zta pro tein was variously modified in different host cells. 311H mAb was gene rated using antigens purified from one-step His-Bind column chromatogr aphy. The antigenic epitope recognized by this mAb was mapped within t he residues 1-152 of EBV DNase by reacting the mAb with three distinct truncated mutants. Also, using 311H as a reagent to trace the kinetic expression of EBV DNase proteins in EBV-infected Akata cells, the Wes tern blotting results indicated that DNase antigen could be detected a t 12 h postactivation. The feasibility of applying these two mAb in th e investigation of EBV biology is discussed.