scholarly journals Phagocytosis and Epithelial Cell Invasion by Crohn’s Disease-Associated Adherent-Invasive Escherichia coli Are Inhibited by the Anti-inflammatory Drug 6-Mercaptopurine

2018 ◽  
Vol 9 ◽  
Author(s):  
Federica Migliore ◽  
Raffaella Macchi ◽  
Paolo Landini ◽  
Moira Paroni
Keyword(s):  
Escherichia Coli ◽  
Crohn’S Disease ◽  
Epithelial Cell ◽  
Crohn's Disease ◽  
Cell Invasion ◽  
Inflammatory Drug ◽  
Anti Inflammatory ◽  
Epithelial Cell Invasion

Nonsteroidal anti-inflammatory drug–induced protein-losing enteropathy: a great masquerade of Crohn’s disease

2017 ◽  
Vol 86 (6) ◽  
pp. 1180-1181 ◽  
Author(s):  
Daniela Guerrero Vinsard ◽  
Mark E. Stark ◽  
Jason T. Lewis ◽  
Ming-Hsi Wang
Keyword(s):  
Crohn’S Disease ◽  
Crohn's Disease ◽  
Drug Induced ◽  
Protein Losing Enteropathy ◽  
Inflammatory Drug ◽  
Anti Inflammatory

scholarly journals Contribution of FliC to Epithelial Cell Invasion by Enterohemorrhagic Escherichia coli O113:H21

2006 ◽  
Vol 74 (12) ◽  
pp. 6999-7004 ◽  
Author(s):  
Shelley N. Luck ◽  
Luminita Badea ◽  
Vicki Bennett-Wood ◽  
Roy Robins-Browne ◽  
Elizabeth L. Hartland
Keyword(s):  
Escherichia Coli ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Invasion ◽  
Intestinal Epithelium ◽  
Enterohemorrhagic Escherichia Coli ◽  
Specific Antibodies ◽  
Epithelial Cell Invasion

ABSTRACT Enterohemorrhagic Escherichia coli (EHEC) O113:H21 can invade epithelial cells. In this study, we found that invasion but not adherence was inhibited by anti-FliCH21 specific antibodies. In addition, deletion of fliCH21 from EHEC O113:H21 resulted in an eightfold decrease in invasion that was restored upon transcomplementation with fliCH21 but not with fliCH6 . These results suggested that FliC plays an important role in the pathogenesis of infections caused by EHEC O113:H21 by allowing bacteria to penetrate the intestinal epithelium.

scholarly journals Epithelial cell invasion by bovine septicemic Escherichia coli.

1994 ◽  
Vol 62 (1) ◽  
pp. 41-47 ◽  
Author(s):  
M J Korth ◽  
J C Lara ◽  
S L Moseley
Keyword(s):  
Escherichia Coli ◽  
Epithelial Cell ◽  
Cell Invasion ◽  
Epithelial Cell Invasion

scholarly journals Escherichia coli O157:H7 Curli Fimbriae Promotes Biofilm Formation, Epithelial Cell Invasion, and Persistence in Cattle

2020 ◽  
Vol 8 (4) ◽  
pp. 580 ◽  
Author(s):  
Haiqing Sheng ◽  
Yansong Xue ◽  
Wei Zhao ◽  
Carolyn J. Hovde ◽  
Scott A. Minnich
Keyword(s):  
Escherichia Coli ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Invasion ◽  
Base Pair ◽  
Biofilm Formation ◽  
Escherichia Coli O157 ◽  
Single Base ◽  
Single Base Pair ◽  
Epithelial Cell Invasion

Escherichia coli O157:H7 (O157) is noninvasive and a weak biofilm producer; however, a subset of O157 are exceptions. O157 ATCC 43895 forms biofilms and invades epithelial cells. Tn5 mutagenesis identified a mutation responsible for both phenotypes. The insertion mapped within the curli csgB fimbriae locus. Screening of O157 strains for biofilm formation and cell invasion identified a bovine and a clinical isolate with those characteristics. A single base pair A to T transversion, intergenic to the curli divergent operons csgDEFG and csgBAC, was present only in biofilm-producing and invasive strains. Using site-directed mutagenesis, this single base change was introduced into two curli-negative/noninvasive O157 strains and modified strains to form biofilms, produce curli, and gain invasive capability. Transmission electron microscopy (EM) and immuno-EM confirmed curli fibers. EM of bovine epithelial cells (MAC-T) co-cultured with curli-expressing O157 showed intracellular bacteria. The role of curli in O157 persistence in cattle was examined by challenging cattle with curli-positive and -negative O157 and comparing carriage. The duration of bovine colonization with the O157 curli-negative mutant was shorter than its curli-positive isogenic parent. These findings definitively demonstrate that a single base pair stably confers biofilm formation, epithelial cell invasion, and persistence in cattle.

scholarly journals Epithelial Cell Adherence Mediated by the Enterotoxigenic Escherichia coli Tia Protein

2000 ◽  
Vol 68 (12) ◽  
pp. 6595-6601 ◽  
Author(s):  
Joseph G. Mammarappallil ◽  
Eric A. Elsinghorst
Keyword(s):  
Escherichia Coli ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Outer Membrane ◽  
Cell Invasion ◽  
Outer Membrane Proteins ◽  
Sodium Dodecyl ◽  
Enterotoxigenic Escherichia Coli ◽  
E Coli ◽  
Epithelial Cell Invasion

ABSTRACT In vitro studies have shown that enterotoxigenic Escherichia coli (ETEC) strains are capable of invading cultured epithelial cells derived from the human ileum and colon. Two separate invasion loci (tia and tib) have previously been isolated from the classical ETEC strain H10407 . The tialocus has been shown to direct the synthesis of Tia, a 25-kDa outer membrane protein. Tia is sufficient to confer the adherence and invasion phenotypes on laboratory stains of E. coli, suggesting that this protein is an adhesin and invasin. Here we report the purification of Tia and characterize its biological activity. Tia was purified by electroelution of outer membrane proteins that had been separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Purified Tia was labeled with biotin and then shown to bind to HCT8 human ileocecal epithelial cells in a specific and saturable manner. Polyclonal anti-Tia antiserum blocked this binding. These results show that Tia acts as an adhesin. Polyclonal anti-Tia antiserum also inhibited invasion of recombinant E. coli bearingtia clones, indirectly suggesting that Tia may also act as an invasin. We predict Tia to contain eight transmembrane amphipathic β-sheets with four loops that are exposed on the surface of the bacterial cell. A peptide corresponding to 19 residues in one of the four predicted surface-exposed loops inhibits Tia-mediated epithelial cell invasion. Seeding HCT8 cells on wells coated with purified Tia reduced Tia-mediated epithelial cell invasion. Together, these results indicate that Tia is an invasin and adhesin that binds a specific receptor on HCT8 cells.

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