A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion

Yixin Fu and Jorge E. Galán ()
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Yixin Fu: Section of Microbial Pathogenesis, Boyer Center for Molecular Medicine, Yale School of Medicine
Jorge E. Galán: Section of Microbial Pathogenesis, Boyer Center for Molecular Medicine, Yale School of Medicine

Nature, 1999, vol. 401, issue 6750, 293-297

Abstract: Abstract An essential feature of the bacterial pathogen Salmonella spp. is its ability to enter cells that are normally non-phagocytic, such as those of the intestinal epithelium1. The bacterium achieves entry by delivering effector proteins into the host-cell cytosol by means of a specialized protein-secretion system (termed type III), which causes reorganization of the cell's actin cytoskeleton and ruffling of its membrane2,3,4. One of the bacterial effectors that stimulates these cellular responses is SopE, which acts as a guanyl-nucleotide-exchange factor on Rho GTPase proteins such as Cdc42 and Rac (ref. 5). As the actin-cytoskeleton reorganization induced by Salmonella is reversible and short-lived, infected cells regain their normal architecture after bacterial internalization6,7. We show here 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. SptP exerts this function by acting as a GTPase-activating protein (GAP) for Rac-1 and Cdc42.

Date: 1999
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DOI: 10.1038/45829

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