MECHANISM OF THE CYTOLYTIC ACTION OF PSEUDOMONAS-AERUGINOSA CYTOTOXIN - OLIGOMERIZATION OF THE CYTOTOXIN ON TARGET MEMBRANES

被引：10

作者：

OHNISHI, M ^{[1
]}

HAYASHI, T ^{[1
]}

TOMITA, T ^{[1
]}

TERAWAKI, Y ^{[1
]}

机构：

[1] UNIV TOKYO,INST MED SCI,MINATO KU,TOKYO 108,JAPAN

来源：

FEBS LETTERS | 1994年 / 356卷 / 2-3期

关键词：

PSEUDOMONAS AERUGINOSA; CYTOTOXIN; PORE FORMATION; OLIGOMERIZATON;

D O I：

10.1016/0014-5793(94)01311-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pseudomonas aeruginosa cytotoxin (CTX) is thought to be a port-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.

引用

页码：357 / 360

页数：4

共 23 条

[1] DAMAGE TO MAMMALIAN-CELLS BY PROTEINS THAT FORM TRANSMEMBRANE PORES [J].