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Infection and Immunity, September 2008, p. 3869-3880, Vol. 76, No. 9
0019-9567/08/$08.00+0     doi:10.1128/IAI.00427-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Escherichia coli DraE Adhesin-Associated Bacterial Internalization by Epithelial Cells Is Promoted Independently by Decay-Accelerating Factor and Carcinoembryonic Antigen-Related Cell Adhesion Molecule Binding and Does Not Require the DraD Invasin{triangledown}

Natalia Korotkova,1 Yuliya Yarova-Yarovaya,2 Veronika Tchesnokova,1 Nina Yazvenko,1 Mike A. Carl,1 Ann E. Stapleton,2 and Steve L. Moseley1*

Department of Microbiology,1 Division of Allergy and Infectious Diseases, University of Washington, Seattle, Washington 98195-72422

Received 6 April 2008/ Returned for modification 8 May 2008/ Accepted 5 June 2008

The Dr family of Escherichia coli adhesins are virulence factors associated with diarrhea and urinary tract infections. Dr fimbriae are comprised of two subunits. DraE/AfaE represents the major structural, antigenic, and adhesive subunit, which recognizes decay-accelerating factor (DAF) and carcinoembryonic antigen (CEA)-related cell adhesion molecules (CEACAMs) CEA, CEACAM1, CEACAM3, and CEACAM6 as binding receptors. The DraD/AfaD subunit caps fimbriae and has been implicated in the entry of Dr-fimbriated E. coli into host cells. In this study, we demonstrate that DAF or CEACAM receptors independently promote DraE-mediated internalization of E. coli by CHO cell transfectants expressing these receptors. We also found that DraE-positive recombinant bacteria adhere to and are internalized by primary human bladder epithelial cells which express DAF and CEACAMs. DraE-mediated bacterial internalization by bladder cells was inhibited by agents which disrupt lipid rafts, microtubules, and phosphatidylinositol 3-kinase (PI3K) activity. Immunofluorescence confocal microscopic examination of epithelial cells detected considerable recruitment of caveolin, β1 integrin, phosphorylated ezrin, phosphorylated PI3K, and tubulin, but not F-actin, by cell-associated bacteria. Finally, we demonstrate that the DraD subunit, previously implicated as an "invasin," is not required for β1 integrin recruitment or bacterial internalization.

* Corresponding author. Mailing address: Department of Microbiology, University of Washington, Box 357242, Seattle, WA 98195-7242. Phone: (206) 543-2820. Fax: (206) 543-8297. E-mail: moseley{at}u.washington.edu

{triangledown} Published ahead of print on 16 June 2008.

Editor: B. A. McCormick

Infection and Immunity, September 2008, p. 3869-3880, Vol. 76, No. 9
0019-9567/08/$08.00+0     doi:10.1128/IAI.00427-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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