Effect of concanavalin A on intracellular killing of Staphylococcus aureus by human phagocytes.

This study concerns the influence of concanavalin A (Con A) on phagocytosis and intracellular killing of Staphylococcus aureus by human monocytes and granulocytes. Con A binds to S. aureus, monocytes, and granulocytes, and is not opsonic. Con A stimulates the killing of intracellular serum opsonized S. aureus by monocytes, but not by granulocytes. This stimulation of intracellular killing was inhibited by alpha-methyl-mannoside, indicating that the process occurs via Con A specific membrane binding sites. Unlike (tetravalent) Con A, divalent succinyl-Con A does not stimulate intracellular killing, indicating that the lectin valency is important for this stimulation. Con A bound to Sephadex particles, that can not be ingested by monocytes, does not stimulate intracellular killing of S. aureus either, although it, like free Con A, stimulates H2O2 production. Pre-incubation of monocytes with Con A inhibited Fc gamma and C3b-mediated ingestion of S. aureus as well as stimulation of the killing by serum. Divalent Con A had no effect on these functions. This inhibition by Con A is in all probability due to a steric impedance of Con A with respect to the interaction of IgG and C3b with their membrane receptors. Fluorescence techniques showed that Con A was localized on the membrane and in the cytoplasm of the monocytes, whereas granulocytes had only membrane bound lectin. Taken together, these findings suggest that cell penetration by the lectin is obligatory for the stimulation of intracellular killing.