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ADP‐ribosylation of cell membrane proteins by staphylococcal α‐toxin and leukocidin in rabbit erythrocytes and polymorphonuclear leukocytes
Author(s) -
Kato Iwao,
Noda Masatoshi
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81060-9
Subject(s) - adp ribosylation , toxin , leukocidin , streptolysin , gtp' , adp ribosylation factor , agmatine , pertussis toxin , g protein , biochemistry , lysis , cytolysis , biology , clostridium difficile toxin a , chemistry , microbiology and biotechnology , staphylococcus aureus , nad+ kinase , cell , receptor , in vitro , bacteria , cytotoxicity , enzyme , putrescine , clostridium difficile , genetics , antibiotics , methicillin resistant staphylococcus aureus , golgi apparatus , bacterial protein , gene
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.