Demonstration of C3b receptor-like activity and of decay-accelerating factor-like activity on rabbit erythrocytes.

C3b receptor activity and decay-accelerating activity for the C3 convertase, C3b,Bb, were demonstrated on rabbit erythrocytes (ERAB). Particles bearing C3b agglutinated ERAB if the C3b was of rabbit origin, but not if it was of human origin. The reactivity of rabbit C3b was abolished by enzymatic conversion of C3b to C3bi. Deposited on ERAB, rabbit C3b, but not human C3b, was cleaved by factor I in the absence of factor H. Similarly, decay acceleration of the C3b,Bb complex on ERAB occurred when the complex was of rabbit origin, but not when it was of human origin. Soluble immune complexes in the presence of rabbit serum were bound to and then released from the ERAB. Binding of the complexes is presumed to be mediated by immune complex-bound C3b and release to be the consequence of degradation of C3b by Factor I. These findings suggest that ERAB, like human erythrocytes, are endowed with membrane-associated complement regulators that protect these cells against homologous complement attack and participate in the clearing mechanism of circulating immune complexes.