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Infection and Immunity, May 2002, p. 2271-2277, Vol. 70, No. 5
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.5.2271-2277.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

A Gene from the Locus of Enterocyte Effacement That Is Required for Enteropathogenic Escherichia coli To Increase Tight-Junction Permeability Encodes a Chaperone for EspF

Simon J. Elliott,1,2 Colin B. O'Connell,3 Athanasia Koutsouris,4 Carl Brinkley,1 Michael S. Donnenberg,3 Gail Hecht,4 and James B. Kaper1*

Center for Vaccine Development and Department of Microbiology and Immunology,1 Division of Infectious Disease, Department of Medicine and Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, Maryland 21201,3 Department of Pediatrics, Division of Infectious Disease, Johns Hopkins University, Baltimore, Maryland 21205,2 Department of Medicine, Section of Digestive and Liver Diseases, University of Illinois, and West Side Veterans Affairs Medical Center, Chicago, Illinois 606124

Received 13 September 2001/ Returned for modification 21 November 2001/ Accepted 23 January 2002

Disruption of the barrier properties of the enterocyte tight junction is believed to be important in the pathogenesis of diarrhea caused by enteropathogenic Escherichia coli (EPEC). This phenotype can be measured in vitro as the ability of EPEC to reduce transepithelial resistance (TER) across enterocyte monolayers and requires the products of the locus of enterocyte effacement (LEE) and, in particular, the type III secreted effector protein EspF. We report a second LEE-encoded gene that is also necessary for EPEC to fully reduce TER. rorf10 is not necessary for EPEC adherence, EspADB secretion, or formation of attaching and effacing lesions. However, rorf10 mutants have a diminished TER phenotype, reduced intracellular levels of EspF, and a reduced ability to translocate EspF into epithelial cells. The product of rorf10 is a 14-kDa intracellular protein rich in {alpha}-helices that specifically interacts with EspF but not with Tir or other EPEC secreted proteins. These properties are consistent with the hypothesis that rorf10 encodes a type III secretion chaperone for EspF, and we rename this protein CesF, the chaperone for EPEC secreted protein F.

* Corresponding author. Mailing address: Center for Vaccine Development, University of Maryland School of Medicine, 685 W. Baltimore St., Baltimore, MD 21201. Phone: (410) 706-2344. Fax: (410) 706-0182. E-mail: jkaper{at}umaryland.edu.

Editor: V. J. DiRita

Infection and Immunity, May 2002, p. 2271-2277, Vol. 70, No. 5
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.5.2271-2277.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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