title: Mechanism of the cytolytic action of Pseudomonas aeruginosa cytotoxin: oligomerization of the cytotoxin on target membranes.
abstract: Pseudomonas aeruginosa cytotoxin (CTX) is thought to be a pore-forming polypeptide of 29 kDa. To study whether CTX assembles into oligomer on target membranes, we solubilized membrane-bound toxin with 1% sodium dodecyl sulfate (SDS) at 25 degrees C and analyzed its molecular size using SDS-polyacrylamide gel electrophoresis and immunoblot analysis. The results indicate that CTX forms a complex of approximately 145 kDa on the surface of erythrocytes and lipid vesicles, and that the complex formation is closely correlated with the toxin-induced permeabilization of target membranes. Thus, CTX may assemble into a pore-forming oligomer on target membranes.
authors: Department of Bacteriology, Shinsyu University School of Medicine, Matsumoto, Japan.
authors: M
authors: M
authors: Ohnishi
authors: T
authors: T
authors: Hayashi
authors: T
authors: T
authors: Tomita
authors: Y
authors: Y
authors: Terawaki
mesh_terms: D000818:Animals; D004305:Dose-Response Relationship, Drug; D004910:Erythrocyte Membrane; D004912:Erythrocytes / Q000187:drug effects; D006461:Hemolysis; D007956:Leukocidins / Q000737:chemistry* / Q000633:toxicity*; D008081:Liposomes; D046911:Macromolecular Substances; D011550:Pseudomonas aeruginosa; D051381:Rats
chemical_list: D007956:Leukocidins; D008081:Liposomes; D046911:Macromolecular Substances