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Infection and Immunity, January 2009, p. 517-531, Vol. 77, No. 1
0019-9567/09/$08.00+0     doi:10.1128/IAI.00695-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Human Decay-Accelerating Factor and CEACAM Receptor-Mediated Internalization and Intracellular Lifestyle of Afa/Dr Diffusely Adhering Escherichia coli in Epithelial Cells{triangledown}

Julie Guignot, Sylvie Hudault, Imad Kansau, Ingrid Chau, and Alain L. Servin*

INSERM, UMR756, Signalisation et Physiopathologie des Cellules Epithéliales, Châtenay-Malabry, France, and Université Paris-Sud 11, Faculté de Pharmacie, Châtenay-Malabry, France

Received 3 June 2008/ Returned for modification 18 July 2008/ Accepted 2 November 2008

We used transfected epithelial CHO-B2 cells as a model to identify the mechanism mediating internalization of Afa/Dr diffusely adhering Escherichia coli. We provide evidence that neither the {alpha}5 or β1 integrin subunits nor {alpha}5β1 integrin functioned as a receptor mediating the adhesion and/or internalization of Dr or Afa-III fimbria-positive bacteria. We also demonstrated that (i) whether or not the AfaD or DraD invasin subunits were present, there was no difference in the cell association and entry of bacteria and that (ii) DraE or AfaE-III adhesin subunits are necessary and sufficient to promote the receptor-mediated bacterial internalization into epithelial cells expressing human decay-accelerating factor (DAF), CEACAM1, CEA, or CEACAM6. Internalization of Dr fimbria-positive E. coli within CHO-DAF, CHO-CEACAM1, CHO-CEA, or CHO-CEACAM6 cells occurs through a microfilament-independent, microtubule-dependent, and lipid raft-dependent mechanism. Wild-type Dr fimbria-positive bacteria survived better within cells expressing DAF than bacteria internalized within CHO-CEACAM1, CHO-CEA, or CHO-CEACAM6 cells. In DAF-positive cells, internalized Dr fimbria-positive bacteria were located in vacuoles that contained more than one bacterium, displaying some of the features of late endosomes, including the presence of Lamp-1 and Lamp-2, and some of the features of CD63 proteins, but not of cathepsin D, and were acidic. No interaction between Dr fimbria-positive-bacterium-containing vacuoles and the autophagic pathway was observed.

* Corresponding author. Mailing address: UMR756, Faculté de Pharmacie, 5 Rue J. B. Clément, 92296 Châtenay-Malabry Cedex, France. Phone: 33-1 46 83 56 61. Fax: 33-1 46 83 58 44. E-mail: alain.servin{at}u-psud.fr

{triangledown} Published ahead of print on 17 November 2008.

Editor: B. A. McCormick

Infection and Immunity, January 2009, p. 517-531, Vol. 77, No. 1
0019-9567/09/$08.00+0     doi:10.1128/IAI.00695-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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