Cytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in Shigella

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Cytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in Shigella.

Type III secretion (T3S) systems are largely used by pathogenic gram-negative bacteria to inject multiple effectors into eukaryotic cells. Upon cell contact, these bacterial microinjection devices insert two T3S substrates into host cell membranes, forming a so-called 'translocon' that is required for targeting of type III effectors in the cell cytosol. Here, we show that secretion of the trans...

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Liposomes recruit IpaC to the Shigella flexneri type III secretion apparatus needle as a final step in secretion induction.

Shigella flexneri contact with enterocytes induces a burst of protein secretion via its type III secretion apparatus (TTSA) as an initial step in cellular invasion. We have previously reported that IpaD is positioned at the TTSA needle tip (M. Espina et al., Infect. Immuno. 74:4391-4400, 2006). From this position, IpaD senses small molecules in the environment to control the presentation of Ipa...

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Induction of necrosis in human neutrophils by Shigella flexneri requires type III secretion, IpaB and IpaC invasins, and actin polymerization.

Infection by Shigella flexneri is characterized by infiltration of neutrophils in the intestinal mucosa and by a strong inflammatory reaction. Although neutrophils are constitutively programmed to die by apoptosis, we show that isolated human neutrophils undergo necrosis 2 h after infection with virulent S. flexneri strain M90T but not with the virulence plasmid-cured strain BS176. This was dem...

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The Tripartite Type III Secreton of Shigella flexneri Inserts Ipab and Ipac into Host Membranes

Bacterial type III secretion systems serve to translocate proteins into eukaryotic cells, requiring a secreton and a translocator for proteins to pass the bacterial and host membranes. We used the contact hemolytic activity of Shigella flexneri to investigate its putative translocator. Hemolysis was caused by formation of a 25-A pore within the red blood cell (RBC) membrane. Of the five protein...

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ژورنال

عنوان ژورنال: The EMBO Journal

سال: 2008

ISSN: 0261-4189,1460-2075

DOI: 10.1038/sj.emboj.7601976