Identification of Epstein-Barr virus strain differences with monoclonal antibody to a membrane glycoprotein.

Two monoclonal antibodies directed against Epstein--Barr virus (EBV)-induced membrane antigens (MA) were isolated in this study. On of the monoclonal antibodies, designated 2F5.6, was an IgG2 which, as detected by membrane and fixed cell immunofluorescence, reacted with MA-positive lymphoblastoid cell lines that produced transforming EBV but not with the MA-positive P3HR-1 cell line that produced the lytic, nontransforming strain of this virus. This antibody precipitated the Mr 320,000/350,000 glycoprotein from B-95 virus infected cultures and the Mr 300,000 and 220,000/250,000 glycoproteins from Raji cells superinfected with P3HR-1 virus but did not precipitate any of these EBV-specific glycoproteins from the P3HR-1 cell line. In contrast, the second monoclonal antibody, IgM designated B10.3, reacted with all virus-producing cell lines including the P3HR-1 cell line. The identity of the glycoprotein that serves as the target for this antibody is still unknown. Neither antibody had neutralizing activity against the B-95 or P3HR-1 strain of EBV. These results indicated that the 2F5.6 monoclonal antibody was directed against an antigenic determinant on the major membrane glycoprotein which is common to transforming strains of EBV but absent from the lytic P3HR-1 stain whereas the B10.3 monoclonal antibody was directed against a group-specific EBV-induced membrane determinant.