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

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Abstract
Staphylococcal α‐toxin resulted in ADP‐ribosylation of the 37 and 41 kDa proteins of a membrane preparation from rabbit erythrocytes. In the presence of 100 μM 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 α‐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 α‐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.