Complement‐mediated adherence of immune complexes to human erythrocytes

Abstract
The classical pathway of complement is required for the adherence of soluble tetanus toxoid (TT)‐human anti‐TT complexes to erythrocytes. Using human C4‐deficient serum we compared the capacity of the two forms of human C4 (C4A and C4B) to mediate this function: C4A was shown to be 1.5‐fold more efficient than C4B. In contrast, haemolysis by C4B was 3.7‐fold more efficient than by C4A. Such large differences suggest that both forms are complementary, and that C4A is preferentially involved in the processing of immune complexes in humans.