Monoclonal antibodies against nuclear antigens, such as DNA, histones, Sm, U1 RNP, and SS-B (La), which are targets of spontaneously occurring autoantibodies in systemic rheumatic diseases, have recently been produced by several investigators (1-5). The significance of using monoclonal antibodies against nuclear autoantigens lies in their monospecificity , as compared with human autoimmune sera, which frequently target more than 1 nuclear antigen (6). Therefore, monoclonal antinuclear antibodies should be important probes not only for standardization of clinical tests, but also for further dissecting the structure and function of reactive antigens. In a recent study, we showed that monoclonal anti-native DNA (anti-nDNA) antibodies also reacted with mitochondrial DNA in tissue culture cells (7). This observation facilitated studies to determine why certain human systemic lupus erythematosus sera that display high titers of anti-nDNA antibodies stain mitochondria in tissue culture cells (7).In the present study, we have shown that a monoclonal autoantibody derived from an autoimmune (New Zealand black X New Zealand white)F1 ([NZB/NZW]F1) mouse reacts with an M , 34,000 nucleolar protein. This protein was demonstrated to share an epitope which is also recognized by scleroderma antibodies reactive with an M , 34,000 nucleolar protein associated with the U3 RNP (8,9).
MATERIALS AND METHODSMonoclonal antibodies. Monoclonal antibodies were produced by hybridoma technology as described previously (10). Splenocytes from a 6-month-old female, unmanipulated (NZBMZW)FI mouse were mixed, at a ratio of lO:l, with nonsecreting myeloma cells (P3x63Ag8.653) and fused with 35% polyethylene glycol. Hybrids were selected in hypoxanthine/aminopteridthymidine-containing medium, as described (10). After propagating hybridomas and subcloning