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© 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

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.

http://www.ncbi.nlm.nih.gov/pubmed/9001387