Studies on the effects of ADP-ribosyltransferase activities of staphylococcal cytolytic toxins on the signal transduction in cell membrane.

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1. 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 muM 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.2. 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.3. 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.4. The S component of staphylococcal leukocidin ADP-ribosylated 37 kDa GTP-binding protein involved in the transduction to activate phospholipase A_<2'> and the F component resulted in ADP-ribosylation of 41 kDa GTP-binding protein involved in the transduction to activate phosphoinositide-specific phospholipase C.