ANTI-RIBOSOMAL ANTIBODIES BIND THE SM PROTEIN-D AND B B'/

In order to analyse the specificity of human anti-ribosomal P protein antibodies, anti-ribosomal P protein antibodies were affinity-purified from the sera of lupus patients. Their binding capacity towards recom binant SmD protein and recombinant SmB/B' protein was evaluated by imm unoblot and ELISA. Epitope mapping of SmD was performed by means of sy nthetic peptides. Anti-ribosomal P protein antibodies bound recombinan t SmD (5/10) and SmB/B' (4/10) on immunoblot; 6/10 showed binding capa city to SmD on ELISA. Inhibition experiments using ELISA confirmed the specificity of this binding. Our data indicate the cross-reactivity o f spontaneously developed anti-ribosomal P protein antibodies with the B/B' and D constituents of the Sm complex. The coexistence of anti-Sm and anti-ribosomal antibodies in lupus sera may therefore be due, at least in part, to the reactivity of a single autoantibody population.