ADP-ribosylation of cell membrane proteins by staphylococcal alpha-toxin and leukocidin in rabbit erythrocytes and polymorphonuclear leukocytes.

Staphylococcal alpha-toxin resulted in ADP-ribosylation of the 37 and 41 kDa proteins of a membrane preparation from rabbit erythrocytes. In the presence of 100 microM GTP, the toxin ADP-ribosylated proteins of 54 and 59 kDa and potentiated ADP-ribosylation of the 37 and 41 kDa forms. GTP had no effect on ADP-ribosylation of membrane proteins in the absence of alpha-toxin. Incubation of a membrane preparation of rabbit polymorphonuclear leukocytes with the S and F components of staphylococcal leukocidin resulted in ADP-ribosylation of the 37 and 41 kDa proteins, respectively. Furthermore, the 37, 41, 54 and 59 kDa proteins were ADP-ribosylated by leukocidin in the presence of GTP. The ADP-ribosylation of these proteins was observed to be dependent on the incubation time and toxin dose and was abolished by prior boiling. Addition of agmatine did not attenuate ADP-ribosylation of these proteins. These results demonstrate that staphylococcal alpha-toxin and leukocidin possess ADP-ribosyltransferase activities which are potentiated by GTP and suggest that ADP-ribosylation reactions are responsible for development of the cytolytic activities of these staphylococcal toxins.