The Brush-Border Adhesion Test for the Assessment of the Adhesive Ability of Escherichia Coli Pathogenic to Pigs, Calves and Lambs

1981 ◽  
pp. 171-174
Author(s):  
P. W. de Leeuw ◽  
P. A. M. Guinée
Keyword(s):  
Escherichia Coli ◽  
Brush Border ◽  
Adhesion Test ◽  
Adhesive Ability

scholarly journals Two Atypical Enteropathogenic Escherichia coli Strains Induce the Production of Secreted and Membrane-Bound Mucins To Benefit Their Own Growth at the Apical Surface of Human Mucin-Secreting Intestinal HT29-MTX Cells

2010 ◽  
Vol 78 (3) ◽  
pp. 927-938 ◽  
Author(s):  
Mônica A. M. Vieira ◽  
Tânia A. T. Gomes ◽  
Antonio J. P. Ferreira ◽  
Terezinha Knöbl ◽  
Alain L. Servin ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Membrane ◽  
Brush Border ◽  
Apical Surface ◽  
Enteropathogenic Escherichia Coli ◽  
Typical Epec ◽  
Membrane Bound

ABSTRACT In rabbit ligated ileal loops, two atypical enteropathogenic Escherichia coli (aEPEC) strains, 3991-1 and 0421-1, intimately associated with the cell membrane, forming the characteristic EPEC attachment and effacement lesion of the brush border, induced a mucous hypersecretion, whereas typical EPEC (tEPEC) strain E2348/69 did not. Using cultured human mucin-secreting intestinal HT29-MTX cells, we demonstrate that apically aEPEC infection is followed by increased production of secreted MUC2 and MUC5AC mucins and membrane-bound MUC3 and MUC4 mucins. The transcription of the MUC5AC and MUC4 genes was transiently upregulated after aEPEC infection. We provide evidence that the apically adhering aEPEC cells exploit the mucins' increased production since they grew in the presence of membrane-bound mucins, whereas tEPEC did not. The data described herein report a putative new virulence phenomenon in aEPEC.

scholarly journals The Escherichia coli Enterotoxin STb Permeabilizes Piglet Jejunal Brush Border Membrane Vesicles

2007 ◽  
Vol 75 (5) ◽  
pp. 2208-2213 ◽  
Author(s):  
Carina Gonçalves ◽  
Vincent Vachon ◽  
Jean-Louis Schwartz ◽  
J. Daniel Dubreuil
Keyword(s):  
Escherichia Coli ◽  
Membrane Potential ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Ionic Selectivity ◽  
Intact Membrane ◽  
Target Membrane ◽  
First Time

ABSTRACT The membrane-permeabilizing ability of the Escherichia coli enterotoxin STb was evaluated using brush border membrane vesicles isolated from piglet jejunum and a membrane-potential-sensitive fluorescent probe, 3,3′-dipropylthiadicarbocyanine iodide. A strong membrane potential was generated by the efflux of K+ ions from the vesicles in the presence of the potassium ionophore valinomycin. Under these conditions, preincubation of the vesicles with STb efficiently depolarized the membrane in a dose-dependent and saturable manner. This activity was independent of pH, however, at least between pH 5.5 and 8.0. On the other hand, in the absence of valinomycin, STb had no significant influence on the measured fluorescence levels, indicating that it was unable to modify the ionic selectivity of the intact membrane. In agreement with the fact that the integrity of the disulfide bridges of STb is known to be essential for its biological activity, a reduced and alkylated form of the toxin was unable to depolarize the membrane in the presence of valinomycin. Furthermore, two previously described poorly active STb mutants, M42S and K22A-K23A, showed no membrane-permeabilizing capacity. These results demonstrate for the first time that STb can permeabilize its target membrane and suggest that it does so by forming nonspecific pores.

scholarly journals Recruitment of CD55 and CD66e Brush Border-Associated Glycosylphosphatidylinositol-Anchored Proteins by Members of the Afa/Dr Diffusely Adhering Family of Escherichia coli That Infect the Human Polarized Intestinal Caco-2/TC7 Cells

2000 ◽  
Vol 68 (6) ◽  
pp. 3554-3563 ◽  
Author(s):  
Julie Guignot ◽  
Isabelle Peiffer ◽  
Marie-Françoise Bernet-Camard ◽  
Douglas M. Lublin ◽  
Christophe Carnoy ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Brush Border ◽  
Intestinal Epithelial Cells ◽  
Binding Capacity ◽  
Deletion Mutants ◽  
Stable Transfection ◽  
Intestinal Epithelial ◽  
Inhibition Assay ◽  
Short Consensus Repeat ◽  
Bacteria Inhibition

ABSTRACT The Afa/Dr family of diffusely adhering Escherichia coli (Afa/Dr DAEC) includes bacteria expressing afimbrial adhesins (AFA), Dr hemagglutinin, and fimbrial F1845 adhesin. We show that infection of human intestinal Caco-2/TC7 cells by the Afa/Dr DAEC strains C1845 and IH11128 is followed by clustering of CD55 around adhering bacteria. Mapping of CD55 epitopes involved in CD55 clustering by Afa/Dr DAEC was conducted using CD55 deletion mutants expressed by stable transfection in CHO cells. Deletion in the short consensus repeat 1 (SCR1) domain abolished Afa/Dr DAEC-induced CD55 clustering. In contrast, deletion in the SCR4 domain does not modify Afa/Dr DAEC-induced CD55 clustering. We show that the brush border-associated glycosylphosphatidylinositol (GPI)-anchored protein CD66e (carcinoembryonic antigen) is recruited by the Afa/Dr DAEC strains C1845 and IH11128. This conclusion is based on the observations that (i) infection of Caco-2/TC7 cells by Afa/Dr DAEC strains is followed by clustering of CD66e around adhering bacteria and (ii) Afa/Dr DAEC strains bound efficiently to stably transfected HeLa cells expressing CD66e, accompanied by CD66e clustering around adhering bacteria. Inhibition assay using monoclonal antibodies directed against CD55 SCR domains, and polyclonal anti-CD55 and anti-CD66e antibodies demonstrate that CD55 and CD66e function as a receptors for the C1845 and IH11128 bacteria. Moreover, using structural draE gene mutants, we found that a mutant in which cysteine replaced aspartic acid at position 54 displayed conserved binding capacity but failed to induce CD55 and CD66e clustering. Taken together, these data give new insights into the mechanisms by which Afa/Dr DAEC induces adhesin-dependent cross talk in the human polarized intestinal epithelial cells by mobilizing brush border-associated GPI-anchored proteins known to function as transducing molecules.

Characterization of intestinal brush border guanylate cyclase activation by Escherichia coli heat-stable enterotoxin

1986 ◽  
Vol 245 (1) ◽  
pp. 51-65 ◽  
Author(s):  
Mohamed M.R. ElDeib ◽  
Charlotte D. Parker ◽  
Trygve L. Veum ◽  
Gene M. Zinn ◽  
Arnold A. White
Keyword(s):  
Escherichia Coli ◽  
Guanylate Cyclase ◽  
Brush Border ◽  
Cyclase Activation ◽  
Heat Stable ◽  
Intestinal Brush Border ◽  
Guanylate Cyclase Activation

Effect of bacterial monoassociation on brush-border enzyme activities in ex-germ-free piglets: comparison of commensal and pathogenic Escherichia coli strains

2006 ◽  
Vol 8 (11) ◽  
pp. 2629-2639 ◽  
Author(s):  
Hana Kozakova ◽  
Jirina Kolinska ◽  
Zdenek Lojda ◽  
Zuzana Rehakova ◽  
Jiri Sinkora ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Brush Border ◽  
Enzyme Activities ◽  
Germ Free ◽  
Pathogenic Escherichia Coli ◽  
Brush Border Enzyme
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