Binding and phagocytosis of sialidase-treated rat erythrocytes by a mechanism independent of opsonins.

Rat peritoneal macrophages bind and phagocytoze homologous sialidase-treated erythrocytes at a rate which is dependent on the amount of sialic acid that has been removed from the cells. Increased binding of erythrocytes is observed after the removal of 10-20% of membrane sialic acid, while for phagocytosis at least 30-40% of this substance must be removed. With Vibrio cholerae sialidase only a partial (80%) hydrolysis of rat erythrocyte sialic acid is possible, whereas Arthrobacter ureafaciens sialidase leads to complete desialylation and therefore causes stronger binding and phagocytosis of the erythrocytes than the V. cholerae enzyme. Preincubation of peritoneal macrophages with sialidase impairs binding and phagocytosis. Experiments were performed to account for the stimulation of binding and phagocytosis observed in the presence of native, homologous serum. However, an involvement of immunoglobulins and complement factors of the classical and alternative pathway in the engulfment process has been excluded. Fibronectin, tuftsin and substance P have no influence, either. On the other hand, peanut agglutinin and Erythrina crystagalli agglutinin are potent stimulators of binding and phagocytosis of sialidase-treated erythrocytes, whereas soybean agglutinin has only little and limulin no influence at all. It is concluded that sialidase-treated erythrocytes, having been bound to the beta-galactose-specific lectin on the macrophage surface, are phagocytozed as a function of their number and binding strength to the macrophages. The influence of native serum and especially of the plant lectins on this process is discussed.