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Deputy Director of Department
Deputy Director of National Reference Center
Deputy Head of Facility
Director of Center
Director of Department
Director of Institute
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Group Leader
Head of Facility
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Honorary President of the Departement
Labex Coordinator

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Studies on ether-phospholipids of vascular smooth muscle cells. Identification of a rapid Ca(2+)-dependent hydrolysis of alkyl-phosphatidylethanolamine promoted by endothelin-l

Comigration of tyrosine hydroxylase- and gonadotropin-releasing hormone-immunoreactive neurons in the nasal area of human embryos

© Research

Publication : FEBS letters

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

Team: Archived: Molecular Microbial Pathogenesis

Member: Claude Parsot

Scientific Fields

Diseases

Organisms

Applications

Technique

Published in FEBS letters - 01 Jan 1997

De Geyter C, Vogt B, Benjelloun-Touimi Z, Sansonetti PJ, Ruysschaert JM, Parsot C, Cabiaux V

Link to Pubmed [PMID] – 9001387

FEBS Lett. 1997 Jan;400(2):149-54

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.

Published on: 01 Jan 1997