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

FEBS Letters

De Geyter, Carine²  Sansonetti, Philippe J¹  Vogt, Bas²  Cabiaux, Véronique²  Ruysschaert, Jean-Marie²  Benjelloun-Touimi, Zineb¹  Parsot, Claude¹ 

[1] Unité de Pathogénie Microbienne Moléculaire, Institut Pasteur, 28 rue du Dr. Roux, 75015 Paris, France;Laboratoire de Chimie Physique des Macromolécules aux Interfaces, CP 206/2, Université Libre de Bruxelles, Boulevard du Triomphe, 1050 Brussels, Belgium

关键词: Invasion;    Membrane interaction;    pH dependence;   

DOI  :  10.1016/S0014-5793(96)01379-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 with 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.

【 授权许可】

Unknown