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MOLECULAR AND CELLULAR PATHOGENESIS

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, Julie Guignot, Alain Barbat, Christophe Carnoy, Steve L. Moseley, Bogdan J. Nowicki, Alain L. Servin, Marie-Françoise Bernet-Camard
Isabelle Peiffer
Institut National de la Santé et de la Recherche Médicale (INSERM), Unité 510, Faculté de Pharmacie Paris XI, F-92296 Châtenay-Malabry, and
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Julie Guignot
Institut National de la Santé et de la Recherche Médicale (INSERM), Unité 510, Faculté de Pharmacie Paris XI, F-92296 Châtenay-Malabry, and
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Alain Barbat
INSERM, Unité 504, F-94407 Villejuif, France;
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Christophe Carnoy
Department of Microbiology, University of Washington, Seattle, Washington 98195-7242; and
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Steve L. Moseley
Department of Microbiology, University of Washington, Seattle, Washington 98195-7242; and
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Bogdan J. Nowicki
Division of Infectious Diseases, Department of Obstetrics and Gynecology, and Department of Microbiology, The University of Texas Medical Branch, Galveston, Texas 77550
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Alain L. Servin
Institut National de la Santé et de la Recherche Médicale (INSERM), Unité 510, Faculté de Pharmacie Paris XI, F-92296 Châtenay-Malabry, and
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Marie-Françoise Bernet-Camard
Institut National de la Santé et de la Recherche Médicale (INSERM), Unité 510, Faculté de Pharmacie Paris XI, F-92296 Châtenay-Malabry, and
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DOI: 10.1128/IAI.68.10.5979-5990.2000
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ABSTRACT

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.

  • Copyright © 2000 American Society for Microbiology
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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, Julie Guignot, Alain Barbat, Christophe Carnoy, Steve L. Moseley, Bogdan J. Nowicki, Alain L. Servin, Marie-Françoise Bernet-Camard
Infection and Immunity Oct 2000, 68 (10) 5979-5990; DOI: 10.1128/IAI.68.10.5979-5990.2000

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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, Julie Guignot, Alain Barbat, Christophe Carnoy, Steve L. Moseley, Bogdan J. Nowicki, Alain L. Servin, Marie-Françoise Bernet-Camard
Infection and Immunity Oct 2000, 68 (10) 5979-5990; DOI: 10.1128/IAI.68.10.5979-5990.2000
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KEYWORDS

Adhesins, Escherichia coli
Escherichia coli
Intestinal Mucosa
Microvilli

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