Premium
Purification of IpaC, a protein involved in entry of Shigella flexneri into epithelial cells and characterization of its interaction with lipid membranes
Author(s) -
De Geyter Carine,
Vogt Bas,
Benjelloun-Touimi Zineb,
Sansonetti Philippe J,
Ruysschaert Jean-Marie,
Parsot Claude,
Cabiaux Véronique
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01379-8
Subject(s) - shigella flexneri , lysis , microbiology and biotechnology , chemistry , vesicle , phagosome , endosome , membrane protein , membrane , cell , biochemistry , biology , escherichia coli , phagocytosis , gene
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.