Mechanism of the cytolytic action of Pseudomonas aeruginosa cytotoxin: Oligomerization of the cytotoxin on target membranes

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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°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.

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