Binding of antibody to the surface of B lymphocytes was shown to involve the Fc piece of the immunoglobulin molecule. This property was not shared equally by all immunoglobulin classes as revealed by direct binding and inhibition studies. Total IgG globulin was found to label cells more heavily than IgM, and IgG1-containing fractions more heavily than IgG2 fractions lacking IgG1. The ability of various purified myeloma proteins to inhibit attachment of antibody to B cells was examined. Pretreatment of B cells with excess IgG2a, IgA, or light chain proteins failed to inhibit, whereas IgG1 proteins and to a lesser extent Ig2b and IgM proteins at the same concentrations did so. At lower protein concentrations, IgG1 myeloma protein alone retained the capacity to inhibit binding. The conclusion was reached that the receptor on B cells for antibody has a marked predilection for the IgG1 class. Although IgM and IgG2b antibody may bind, they do so with lower avidity and probably in insignificant amounts if IgG1 antibody is present in excess.
No evidence was found to implicate complement in the binding process. For example, heat-inactivated sera at high dilution retained the ability to label B cells, while the use of purified low molecular weight anticomplementary factor, a potent inhibitor of C'3, did not interfere with the formation of the bond between antibody and cell surface.
The failure of anti-mouse immunoglobulin F(ab)'2 fragments to prevent access of antibody to B cells implied that the antibody-binding receptor and antigen-binding (immunoglobulin) receptor are discrete entities on the B cell membrane. Despite this, a marked similarity between their surface distribution was observed on electron microscopy.
The antibody-binding receptor was shown to be a marker for mature B cells. It did not appear to be present on hematopoietic precursor stem cells and was lost during differentiation to antibody-forming cells.