Afa/Dr diffusely adhering Escherichia coli C1845 infection promotes selective injuries in the junctional domain of polarized human intestinal Caco-2/TC7 cells.
The Afa/Dr diffusely adhering Escherichia coli (DAEC) C1845 strain harboring the F1845 fimbrial adhesin interacts with the brush border-associated CD55 molecule and promotes elongation of brush border microvilli resulting from rearrangement of the F-actin network. This phenomenon involves the activation of a cascade of signaling coupled to the glycosylphosphatidylinositol-anchored receptor of the F1845 adhesin. We provide evidence that infection of the polarized human intestinal cell line Caco-2/TC7 by strain C1845 is followed by an increase in the paracellular permeability for [(3)H]mannitol without a decrease of the transepithelial resistance of the monolayers. Alterations in the distribution of tight-junction (TJ)-associated occludin and ZO-1 protein are observed, whereas the distribution of the zonula adherens-associated E-cadherin is not affected. Using the recombinant E. coli strains HB101(pSSS1) and -(pSSS1C) expressing the F1845 fimbrial adhesin, we demonstrate that the adhesin-CD55 interaction is not sufficient for the induction of structural and functional TJ lesions. Moreover, using the actin filament-stabilizing agent Jasplakinolide, we demonstrate that the C1845-induced functional alterations in TJs are independent of the C1845-induced apical cytoskeleton rearrangements. The results indicated that pathogenic factor(s) other than F1845 adhesin may be operant in Afa/Dr DAEC C1845.
Peiffer
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I
Unité 510, Institut National de la Santé et de la Recherche Médicale, Faculté de Pharmacie Paris XI, F-92296 Châtenay-Malabry, France.
Blanc-Potard
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AB
Bernet-Camard
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MF
Guignot
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J
Barbat
A
A
Servin
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AL
D018830:Adhesins, Escherichia coli / Q000235:genetics / Q000378:metabolism; D000942:Antigens, Bacterial; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D018958:CD55 Antigens / Q000378:metabolism; D018938:Caco-2 Cells; D015820:Cadherins / Q000302:isolation & purification; D016764:Cell Polarity; D003599:Cytoskeleton / Q000473:pathology; D004926:Escherichia coli / Q000472:pathogenicity*; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism / Q000382:microbiology* / Q000473:pathology*; D008565:Membrane Proteins / Q000302:isolation & purification; D008954:Models, Biological; D062793:Occludin; D010539:Permeability; D010750:Phosphoproteins / Q000302:isolation & purification; D019108:Tight Junctions / Q000378:metabolism / Q000473:pathology*; D062826:Zonula Occludens-1 Protein
D018830:Adhesins, Escherichia coli; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D018958:CD55 Antigens; D015820:Cadherins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C568985:OCLN protein, human; D062793:Occludin; D010750:Phosphoproteins; C569042:TJP1 protein, human; D062826:Zonula Occludens-1 Protein; C080952:DaaE protein, E coli; D036781:Fimbriae Proteins