Receptors for human gamma G globulin on human neutrophils.

Abstract

Cell surface receptors for human gammaG antibodies directed against bacterial antigens were demonstrated on human neutrophils using an in vitro bacteriocidal-phagocytic assay. These results were confirmed by adherence of sensitized erythrocytes to monolayers of neutrophils or monocytes. Erythrocytes sensitized indirectly with antibacterial gammaG antibodies after passive sensitization with bacterial antigens adhered to both neutrophils and monocytes. Erythrocytes sensitized directly with conventional anti-D gammaG antibodies adhered only to monocytes, while those sensitized with the hyperimmune anti-CD gammaG antibody Ripley adhered to both monocytes and neutrophils. Adherence of anti-Rh or antibacterial gammaG antibodies to monocytes and neutrophils could be inhibited by whole gammaG, myeloma globulins of the gamma(1) or gamma(3) subclasses, or Fc fragments, but not by Fab fragment. These results indicate that receptors for the Fc portion of human gammaG antibodies exist on both neutrophils and monocytes, and that gammaG antibodies differ in their ability to attach to these two cell types. Differences in the behavior of the gammaG antibodies studied may be related to differences in the density of antibodies on the erythrocyte surface and receptors on the phagocytic cells.