Properties of a second epitope of the murine Fc receptor for aggregated IgG

The murine macrophage and lymphocyte Fc receptor for aggregated IgC(FcγR) has previously been characterized by using the anti-FcγR monoclonal antibody (mAb), 2.4G2. In the studies presented here, the authors describe a new mAb, 6B7C, that defines a second epitope of the FcγR. The tissue distribution of the 6B7C epitope is coincident with the 2.4G2 epitope. However, only the 2.4G2 epitope is accessible to mAb binding on intact primary macrophages or lymphocytes. The 6B7C epitope is not detectable on primary macrophages or lymphocytes but is exposed on a portion of B lymphocyte FcγR after activation by lipopolysaccharide and on some tumor cell lines. The expression of the 6B7C epitope on the surface of B lymphoblasts and tumor cell lines seems to correlate with their ability to release soluble FcγR. The 6B7C mAb has the advantage that it reacts with native as well as denatured receptor and therefore can be used for techniques such as immunoblotting. The binding assay was done using 125I-labeled Ig