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

FEBS Letters

Ohnishi, Makoto¹  Terawaki, Yoshiro¹  Hayashi, Tetsuya¹  Tomita, Toshio² 

[1] Department of Bacteriology, Shinsyu University School of Medicine, 3-1-1 Asahi, Matsumoto 390, Japan;The Institute of Medical Science, The University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108, Japan

关键词: Pseudomonas aeruginosa;    Cytotoxin;    Pore formation;    Oligomerizaton;   

DOI  :  10.1016/0014-5793(94)01311-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown