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Journal of Bacteriology, September 2002, p. 4699-4708, Vol. 184, No. 17
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.17.4699-4708.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Salmonella Type III Secretion-Associated Protein InvE Controls Translocation of Effector Proteins into Host Cells

Section of Microbial Pathogenesis, Yale School of Medicine, New Haven, Connecticut 06536

Received 21 March 2002/ Accepted 5 June 2002

Salmonella enterica encodes a type III secretion system (TTSS) within a pathogenicity island located at centisome 63 (SPI-1), which is essential for its pathogenicity. This system mediates the transfer of a battery of bacterial proteins into the host cell with the capacity to modulate cellular functions. The transfer process is dependent on the function of protein translocases SipB, SipC, and SipD. We report here that Salmonella protein InvE, which is also encoded within SPI-1, is essential for the translocation of bacterial proteins into host cells. An S. enterica serovar Typhimurium mutant carrying a loss-of-function mutation in invE shows reduced secretion of SipB, SipC, and SipD while exhibiting increased secretion of other TTSS effector proteins. We also demonstrate that InvE interacts with a protein complex formed by SipB, SipC, and their cognate chaperone, SicA. We propose that InvE controls protein translocation by regulating the function of the Sip protein translocases.

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