Interactions of C-reactive protein with lymphoid cells.

The interactions between CRP and peripheral blood lymphocytes were investigated. CRP, in the presence of an appropriate ligand, bound saturably to a small percentage of normal PBL. The characteristics and optimal conditions for this binding were defined using several different assay systems. CRP was found to bind preferentially to cells with the IgG FcR. Binding was increased in the presence of acute phase sera, and higher numbers of cells binding CRP were observed in acute phase individuals. CRP and CRP-CPS had minimal effects upon lymphocyte responsiveness in vitro, although enhancing effects on MLC and CMC reactions, and a slight blastogenic effect, were observed. CRP antigenicity was detected on a small percentage of PBL, and treatment of PBL with anti-CRP and complement led to loss of NK reactivity, suggesting a possible association of CRP with this function. The functional expression of binding of CRP complexes, the relationship of the CRP-binding site to surface CRP antigenicity and the FcR, and the role of these factors in lymphocyte functions such as NK reactivity and recognition, are yet to be determined.