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Journal of Bacteriology, February 2009, p. 815-821, Vol. 191, No. 3
0021-9193/09/$08.00+0 doi:10.1128/JB.00989-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

and
Marcia B. Goldberg*
Division of Infectious Diseases, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Cambridge, Massachusetts 02139
Received 17 July 2008/ Accepted 18 November 2008
IcsA is an outer membrane protein in the autotransporter family that is required for Shigella flexneri pathogenesis. Following its secretion through the Sec translocon, IcsA is incorporated into the outer membrane in a process that depends on YaeT, a component of an outer membrane β-barrel insertion machinery. We investigated the role of the periplasmic chaperone Skp in IcsA maturation. Skp is required for the presentation of the mature amino terminus (alpha-domain) of IcsA on the bacterial surface and contributes to cell-to-cell spread of S. flexneri in cell culture. A mutation in skp does not prevent the insertion of the β-barrel into the outer membrane, suggesting that the primary role of Skp is the folding of the IcsA alpha-domain. In addition, the requirement for skp can be partially bypassed by disrupting icsP, an ortholog of Escherichia coli ompT, which encodes the protease that processes IcsA between the mature amino terminus and the β-barrel outer membrane anchor. These findings are consistent with a model in which Skp plays a critical role in the chaperoning of the alpha-domain of IcsA during transit through the periplasm.
Published ahead of print on 1 December 2008.
Present address: Department of Periodontics, University of Washington, Seattle, WA 98195.
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