scholarly journals Campylobacter jejuniouter membrane vesicle-associated proteolytic activity promotes bacterial invasion by mediating cleavage of intestinal epithelial cell E-cadherin and occludin

2015 ◽  
Vol 18 (4) ◽  
pp. 561-572 ◽  
Author(s):  
Abdi Elmi ◽  
Fauzy Nasher ◽  
Heena Jagatia ◽  
Ozan Gundogdu ◽  
Mona Bajaj-Elliott ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Proteolytic Activity ◽  
Intestinal Epithelial Cell ◽  
Membrane Vesicle ◽  
Bacterial Invasion ◽  
Intestinal Epithelial ◽  
E Cadherin

scholarly journals Bacteroides fragilis toxin stimulates intestinal epithelial cell shedding and  -secretase-dependent E-cadherin cleavage

2007 ◽  
Vol 120 (20) ◽  
pp. 3713-3713
Author(s):  
S. Wu ◽  
K.-J. Rhee ◽  
M. Zhang ◽  
A. Franco ◽  
C. L. Sears
Keyword(s):  
Epithelial Cell ◽  
Intestinal Epithelial Cell ◽  
Bacteroides Fragilis ◽  
Intestinal Epithelial ◽  
Cell Shedding ◽  
E Cadherin

scholarly journals Bacteroides fragilis toxin stimulates intestinal epithelial cell shedding and  -secretase-dependent E-cadherin cleavage

2007 ◽  
Vol 120 (11) ◽  
pp. 1944-1952 ◽  
Author(s):  
S. Wu ◽  
K.-J. Rhee ◽  
M. Zhang ◽  
A. Franco ◽  
C. L. Sears
Keyword(s):  
Epithelial Cell ◽  
Intestinal Epithelial Cell ◽  
Bacteroides Fragilis ◽  
Intestinal Epithelial ◽  
Cell Shedding ◽  
E Cadherin

scholarly journals The Bacteroides fragilis Toxin Binds to a Specific Intestinal Epithelial Cell Receptor

2006 ◽  
Vol 74 (9) ◽  
pp. 5382-5390 ◽  
Author(s):  
Shaoguang Wu ◽  
Jai Shin ◽  
Guangming Zhang ◽  
Mitchell Cohen ◽  
Augusto Franco ◽  
...  
Keyword(s):  
Biological Activity ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Intestinal Epithelial Cell ◽  
Intestinal Epithelial Cells ◽  
Cellular Receptor ◽  
Intestinal Epithelial ◽  
Protease Activated Receptors ◽  
E Cadherin

ABSTRACT The Bacteroides fragilis toxin (BFT) is the only known virulence factor of enterotoxigenic B. fragilis. BFT has previously been shown to act, at least in part, through cleavage of the intercellular adhesion protein E-cadherin. A specific cellular receptor for BFT has not been identified. The goal of this study was to determine if the initial interaction of BFT with intestinal epithelial cells was consistent with binding to a specific cellular receptor. Purified BFT was labeled with a fluorophore or iodide to assess specific cellular binding and the properties of BFT cellular binding. BFT binds specifically to intestinal epithelial cell lines in vitro in a polarized manner. However, specific binding occurs only at 37°C and requires BFT metalloprotease activity. The BFT receptor is predicted to be a membrane protein other than E-cadherin or a known protease-activated receptor (PAR1 to PAR4). BFT binding is resistant to acid washing, suggesting an irreversible interaction. Sugar or lipid residues do not appear to be involved in the mechanism of BFT cellular binding, but binding is sensitive to membrane cholesterol depletion. We conclude that intestinal epithelial cells in vitro possess a specific membrane BFT receptor that is distinct from E-cadherin. The data favor a model in which the metalloprotease domain of BFT processes its receptor protein, initiating cellular signal transduction that mediates the biological activity of BFT. However, activation of recognized protease-activated receptors does not mimic or block BFT biological activity or binding, suggesting that additional protease-activated receptors on intestinal epithelial cells remain to be identified.

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