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A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
It is shown that the S. Typhimurium effector protein SptP, which is delivered to the host-cell cytosol by the type-III secretion system, is directly responsible for the reversal of the actin cytoskeletal changes induced by the bacterium.
Salmonella interactions with host cells: type III secretion at work.
  • J. Galán
  • Biology
    Annual review of cell and developmental biology
  • 2001
The bacterial pathogen Salmonella enterica has evolved a very sophisticated functional interface with its vertebrate hosts. At the center of this interface is a specialized organelle, the type III
Type III secretion machines: bacterial devices for protein delivery into host cells.
Several Gram-negative pathogenic bacteria have evolved a complex protein secretion system termed type III to deliver bacterial effector proteins into host cells that then modulate host cellular
Cloning and molecular characterization of genes whose products allow Salmonella typhimurium to penetrate tissue culture cells.
Using an in vitro system, a genetic locus is isolated that confers to a noninvasive strain of Salmonella typhimurium the ability to penetrate tissue culture cells and show decreased ability to colonize the Peyer's patches, the small intestinal wall, and the spleen when administered perorally and intraperitoneally.
Protein delivery into eukaryotic cells by type III secretion machines
A bacterial organelle that has specifically evolved to deliver bacterial proteins into eukaryotic cells is encoded by a large number of bacterial species that are symbiotic or pathogenic for humans, other animals including insects or nematodes, and plants.
RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems
Rip2 is therefore a signal transducer and integrator of signals for both the innate and adaptive immune systems.
A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein.
CdtB mutants with substitutions in residues equivalent to those required for catalysis or magnesium binding in type I deoxyribonucleases did not cause chromatin disruption, and CDT holotoxin containing these mutant forms of CdtB did not induce morphological changes or cell cycle arrest.