In this study monoclonal antibody to Epstein-Barr virus(EBV)-associated antigen was produced and the characteristics and functions of the antigen were investigated. An antibody secreting hybrid cell line was produced by fusion of mouse myeloma
cells(V653) with splenocytes from mice immunized with extracts of TPA treated, EBV producer B95-8 cells. The monoclonal atibody reacted strongly with cytoplasmic membrane and cytoplasm of b95-8 cells and EBV-transformed B lymphoblastoid cell
line(BLCL)
by indirect immunofluorescence test, but EBV genome positive, non-producer Raji cells showed negative reaction to that antibody. The antigen being recognized was characterized by immuno-precipitation of B95-8 cell lysates and SDS-PAGE procedure.
Molecules with estimated molecular weight of 53,000 and 28,000 were identified. By the result of indirect immunofluorescence test and molecular weight estimation, the antigen reacted with this monoclonal antibody presumed to be early antigen
(EA).
Netralization of EBV and blocking of viral release from P95-8 cells when treated with the monoclonal antibody was not observed in transformation of cord blood mononuclear cells and [3H] thymoidine incorporation assay. By TPA treatment viral
production
was increased markedly compared to TPA untreated control group. Regardless of TPA treatment, BLCL showed EBV production. But, TPA treated BLCL showed increased colony fomation in the cultured wells compared to TPA untreated BLCL. Healthy cultured
BLCL
supernatant did not show differences in the colony formation compared to old cultured BLCL supernatant.
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