Influence of processing by erythrocyte C3b/C4b receptors (CR1) on binding of immune complexes to Raji cells and polymorphonuclear granulocytes.

The binding of 125I-labelled bovine serum albumin (BSA)-anti-BSA immune complexes (IC) to Raji cells and polymorphonuclear (PMN) cells in vitro was studied. The IC were reacted for 1 h at 37 degrees C with normal human serum (NHS) diluted 1:2 in the presence or absence of human erythrocytes (E) before presentation for Raji cells or PMN cells. The IC showed a two to three fold increased binding to C3d, g receptors (CR2) on Raji cells, when E-CR1 had been present during the reaction with NHS, compared to IC similarly reacted with NHS only. Blocking of the E-CR1 by a polyclonal anti-CR1 antibody reduced the subsequent binding of IC to Raji cells to the same level as that obtained with IC reacted with serum only. Binding to PMN granulocytes of IC reacted with NHS in the presence of E-CR1 showed a 60% reduction compared to the binding of IC reacted with NHS only. It is concluded that interaction of complement-reacted IC with CR1 on erythrocytes leads to a more efficient generation of CR2-binding C3d, g-containing IC with reduced reactivity to PMN cells.