The human Fc receptor for mouse IgG2b on monocytes and EBV-B cells is functionally inhibited by anti-HLA class II antibodies.

We have recently described a polymorphic Fc receptor for murine IgG2b (mIgG2b), present on human monocytes and EBV-transformed B lymphocytes. The present study shows that anti-HLA class II monoclonal antibody (MoAb) completely inhibits both the (Fc receptor-dependent) T-cell proliferation, induced by mIgG2b anti-CD3 MoAb, and rosetting with mIgG2b-sensitized erythrocytes. This inhibition is also observed with F(ab')2 fragments of anti-HLA class II MoAb, and is therefore not Fc mediated. The Fc receptor for mIgG2b is also present on EBV-transformed B cells obtained from a patient with 'bare lymphocyte syndrome', that completely lack HLA class II antigens. Therefore, the Fc receptor for mIgG2b and HLA class II antigens are not identical. Since the low affinity receptor for IgE (Fc epsilon II; CD23) was reported to be associated at the cell surface with HLA class II antigens, we have compared both types of Fc receptor, and observed that human IgE strongly inhibits the mitogenic effect of murine IgE anti-CD3 but not of mIgG2b anti-CD3 MoAb. We conclude that the human Fc receptor for mIgG2b is strongly inhibited by anti-HLA class II MoAb, but is not identical to HLA class II or Fc epsilon RII.