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Infection and Immunity, October 2000, p. 5979-5990, Vol. 68, No. 10
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Structural and Functional Lesions in Brush Border of Human Polarized Intestinal Caco-2/TC7 Cells Infected by Members of the Afa/Dr Diffusely Adhering Family of Escherichia coli

Isabelle Peiffer,1 Julie Guignot,1 Alain Barbat,2 Christophe Carnoy,3 Steve L. Moseley,3 Bogdan J. Nowicki,4 Alain L. Servin,1,* and Marie-Françoise Bernet-Camard1

Institut National de la Santé et de la Recherche Médicale (INSERM), Unité 510, Faculté de Pharmacie Paris XI, F-92296 Châtenay-Malabry,1 and INSERM, Unité 504, F-94407 Villejuif,2 France; Department of Microbiology, University of Washington, Seattle, Washington 98195-72423; and Division of Infectious Diseases, Department of Obstetrics and Gynecology, and Department of Microbiology, The University of Texas Medical Branch, Galveston, Texas 775504

Received 14 February 2000/Returned for modification 31 May 2000/Accepted 5 July 2000

Diffusely adhering Escherichia coli (DAEC) strains expressing F1845 fimbrial adhesin or Dr hemagglutinin belonging to the Afa/Dr family of adhesins infect cultured polarized human intestinal cells through recognition of the brush border-associated decay-accelerating factor (DAF; CD55) as a receptor. The wild-type Afa/Dr DAEC strain C1845 has been shown to induce brush border lesions by an adhesin-dependent mechanism triggering apical F-actin rearrangements. In the present study, we undertook to further characterize cell injuries following the interaction of wild-type Afa/Dr DAEC strains C1845 and IH11128 expressing fimbrial F1845 adhesin and Dr hemagglutinin, respectively, with polarized, fully differentiated Caco-2/TC7 cells. In both cases, bacterium-cell interaction was followed by rearrangement of the major brush border-associated cytoskeletal proteins F-actin, villin, and fimbrin, proteins which play a pivotal role in brush border assembly. In contrast, distribution of G-actin, actin-depolymerizing factor, and tubulin was not modified. Using draE mutants, we found that a mutant in which cysteine replaces aspartic acid at position 54 conserved binding capacity but failed to induce F-actin disassembly. Accompanying the cytoskeleton injuries, we found that the distribution of brush border-associated functional proteins sucrase-isomaltase (SI), dipeptidylpeptidase IV (DPPIV), glucose transporter SGLT1, and fructose transporter GLUT5 was dramatically altered. In parallel, SI and DPPIV enzyme activity decreased.

* Corresponding author. Mailing address: INSERM Unité 510, Faculté de Pharmacie Paris XI, F-92296 Châtenay-Malabry, France. Phone and fax: 33.1.46.83.56.61. E-mail: alain.servin{at}cep.u-psud.fr.

Infection and Immunity, October 2000, p. 5979-5990, Vol. 68, No. 10
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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