The major receptor for C-reactive protein on leukocytes is Fcγ receptor II

C-reactive protein (CRP) is an acute phase serum protein that shares several functions with immunoglobulin (Ig)G including complement activation and binding to receptors on monocytes and neutrophils. The identity of the receptor for CRP has been the target of extensive research. We previously determined that CRP binds to the high affinity receptor for IgG, Fc gamma RI (CD64). However, this interaction could not account for the majority of binding of CRP to neutrophils or monocytic cells. We now determine that CRP also interacts with Fc gamma RIIa (CD32), the low affinity receptor for IgG on monocytes and neutrophils. COS-7 cells were transfected with a construct containing the human Fc gamma RIIA cDNA. CRP binding and the presence of CD32 were detected by mAb and analyzed by two-color now cytometry. Cells ex pressing CD32 bound CRP in a pose-dependent and saturable manner consistent with receptor binding. CRP bound to transfectants and K-52 cells with similar kinetics, and in both cases binding was completely inhibited by aggregated IgG. On monocytic cell lines, treatment with Bt(2)cAMP increased Fc gamma RII expression and enhanced CRP binding. CRP also specifically precipitated Fc gamma RI and Fc gamma RII from the monocytic cell line, THP-1. It is suggested that the major receptor for CRP on phagocytic cells is Fc gamma RII.