Purification of IpaC, a protein involved in entry of Shigella flexneri into epithelial cells and characterization of its interaction with lipid membranes

被引：45

作者：

DeGeyter, C

Vogt, B

BenjellounTouimi, Z

Sansonetti, PJ

Ruysschaert, JM

Parsot, C

Cabiaux, V

机构：

[1] FREE UNIV BRUSSELS, CHIM PHYS MACROMOL INTERFACES LAB, B-1050 BRUSSELS, BELGIUM

[2] INST PASTEUR, UNITE PATHOGENIE MICROBIENNE MOL, F-75015 PARIS, FRANCE

来源：

FEBS LETTERS | 1997年 / 400卷 / 02期

关键词：

invasion; membrane interaction; pH dependence;

D O I：

10.1016/S0014-5793(96)01379-8

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：

Entry of Shigella flexneri into epithelial cells and lysis of the phagosome involve the secreted IpaA-D proteins. A complex containing IpaC and IpaB is able to promote uptake of inert particles by epithelial cells. This suggested that Ipa proteins, either individually or as a complex, might interact,vith the cell membrane. We have purified IpaC and demonstrated its interaction with lipid vesicles. This interaction is modulated by the pH, which might be relevant to the dual role of Ipa proteins, in induction of membrane ruffles upon entry and lysis of the endosome membrane thereafter.

引用

页码：149 / 154

页数：6

共 30 条

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