Document Detail


Enteropathogenic Escherichia coli inhibits ileal sodium-dependent bile acid transporter ASBT.
MedLine Citation:
PMID:  22403793     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Apical sodium-dependent bile acid transporter (ASBT) is responsible for the absorption of bile acids from the intestine. A decrease in ASBT function and expression has been implicated in diarrhea associated with intestinal inflammation. Whether infection with pathogenic microorganisms such as the enteropathogenic Escherichia coli (EPEC) affect ASBT activity is not known. EPEC is a food-borne enteric pathogen that translocates bacterial effector molecules via type three secretion system (TTSS) into host cells and is a major cause of infantile diarrhea. We investigated the effects of EPEC infection on ileal ASBT function utilizing human intestinal Caco2 cells and HEK-293 cells stably transfected with ASBT-V5 fusion protein (2BT cells). ASBT activity was significantly inhibited following 60 min infection with EPEC but not with nonpathogenic E. coli. Mutations in bacterial escN, espA, espB, and espD, the genes encoding for the elements of bacterial TTSS, ablated EPEC inhibitory effect on ASBT function. Furthermore, mutation in the bacterial BFP gene encoding for bundle-forming pili abrogated the inhibition of ASBT by EPEC, indicating the essential role for bacterial aggregation and the early attachment. The inhibition by EPEC was associated with a significant decrease in the V(max) of the transporter and a reduction in the level of ASBT on the plasma membrane. The inhibition of ASBT by EPEC was blocked in the presence of protein tyrosine phosphatase inhibitors. Our studies provide novel evidence for the alterations in the activity of ASBT by EPEC infection and suggest a possible effect for EPEC in influencing intestinal bile acid homeostasis.
Authors:
Fadi Annaba; Zaheer Sarwar; Ravinder K Gill; Amit Ghosh; Seema Saksena; Alip Borthakur; Gail A Hecht; Pradeep K Dudeja; Waddah A Alrefai
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-03-08
Journal Detail:
Title:  American journal of physiology. Gastrointestinal and liver physiology     Volume:  302     ISSN:  1522-1547     ISO Abbreviation:  Am. J. Physiol. Gastrointest. Liver Physiol.     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-05-16     Completed Date:  2012-07-20     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  100901227     Medline TA:  Am J Physiol Gastrointest Liver Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  G1216-22     Citation Subset:  IM    
Affiliation:
Section of Digestive Diseases and Nutrition, Department of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA.
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MeSH Terms
Descriptor/Qualifier:
Bacterial Outer Membrane Proteins / genetics
Bacterial Secretion Systems / genetics,  physiology
Caco-2 Cells
Enteropathogenic Escherichia coli / drug effects,  genetics,  metabolism*
Enzyme Inhibitors / pharmacology
Escherichia coli Infections / genetics,  metabolism*
Escherichia coli Proteins / genetics,  metabolism
HEK293 Cells
Humans
Mutation
Organic Anion Transporters, Sodium-Dependent / metabolism*
Protein Tyrosine Phosphatases / antagonists & inhibitors
Sodium / metabolism*
Symporters / metabolism*
Grant Support
ID/Acronym/Agency:
DK-050694/DK/NIDDK NIH HHS; DK-058964/DK/NIDDK NIH HHS; DK-54016/DK/NIDDK NIH HHS; DK-71596/DK/NIDDK NIH HHS; DK-74458/DK/NIDDK NIH HHS; DK-81858/DK/NIDDK NIH HHS; P01 DK067887/DK/NIDDK NIH HHS; P01-DK-067887/DK/NIDDK NIH HHS; R01 DK054016/DK/NIDDK NIH HHS; R01 DK081858/DK/NIDDK NIH HHS; R01 DK092441/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/EaeB protein, E coli; 0/Enzyme Inhibitors; 0/Escherichia coli Proteins; 0/EspA protein, E coli; 0/EspD protein, E coli; 0/Organic Anion Transporters, Sodium-Dependent; 0/Symporters; 145420-23-1/sodium-bile acid cotransporter; 7440-23-5/Sodium; EC 3.1.3.48/Protein Tyrosine Phosphatases
Comments/Corrections

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