Premium
IpgD, a protein secreted by the type III secretion machinery of Shigella flexneri , is chaperoned by IpgE and implicated in entry focus formation
Author(s) -
Niebuhr Kirsten,
Jouihri Noureddine,
Allaoui Abdelmounaaim,
Gou Pierre,
Sansonetti Philippe J.,
Parsot Claude
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.02041.x
Subject(s) - biology , secretion , shigella flexneri , effector , cytoplasm , type three secretion system , microbiology and biotechnology , virulence , extracellular , chaperone (clinical) , transport protein , secretory protein , shigella , bacteria , gene , escherichia coli , salmonella , genetics , biochemistry , medicine , pathology
Invasion of epithelial cells by Shigella flexneri involves entry and intercellular dissemination. Entry of bacteria into non‐phagocytic cells requires the IpaA–D proteins that are secreted by the Mxi–Spa type III secretion machinery. Type III secretion systems are found in several Gram‐negative pathogens and serve to inject bacterial effector proteins directly into the cytoplasm of host cells. In this study, we have analysed the IpgD protein of S. flexneri , the gene of which is located on the virulence plasmid at the 5′ end of the mxi–spa locus. We have shown that IpgD (i) is stored in the bacterial cytoplasm in association with a specific chaperone, IpgE; (ii) is secreted by the Mxi–Spa type III secretion system in amounts similar to those of the IpaA–D proteins; (iii) is associated with IpaA in the extracellular medium; and (iv) is involved in the modulation of the host cell response after contact of the bacterium with epithelial cells. This suggests that IpgD is an effector that might be injected into host cells to manipulate cellular processes during infection.