Photolabeling of staphylococcal alpha-toxin from within rabbit erythrocyte membranes.
Intrinsic membrane proteins of rabbit red blood cells were labeled with the photoreactive amphipatic reagent 12-(4-azido-2-nitrophenoxy) stearoyl (1-14C) glucosamine, which inserts into the hydrophobic membrane region and generates a reactive nitrene upon ultraviolet irradiation. Photolabeling of membrane-bound staphylococcal alpha-toxin after lysis of probe-treated rabbit red blood cells by this toxin implies its penetration into the hydrophobic region of the outer leaflet of the membrane. In contrast clostridial theta-toxin and staphylococcal delta-toxin were not labeled, but extraction of intrinsic membrane proteins by delta-toxin was evidenced.
D000818:Animals; D001386:Azides; D001427:Bacterial Toxins / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000187:drug effects*; D004912:Erythrocytes / Q000187:drug effects*; D006460:Hemolysin Proteins; D006461:Hemolysis; D008565:Membrane Proteins / Q000032:analysis; D010777:Photochemistry; D011817:Rabbits
D001386:Azides; D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D008565:Membrane Proteins; C021091:staphylococcal alpha-toxin; C025971:staphylococcal delta toxin; C019266:12-(4-azido-2-nitrophenoxy)stearoylglucosamine; C020452:Clostridium perfringens theta-toxin