Document Detail


Release of metabolic enzymes by Giardia in response to interaction with intestinal epithelial cells.
MedLine Citation:
PMID:  18359106     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Giardia lamblia, an important cause of diarrheal disease, resides in the small intestinal lumen in close apposition to epithelial cells. Since the disease mechanisms underlying giardiasis are poorly understood, elucidating the specific interactions of the parasite with the host epithelium is likely to provide clues to understanding the pathogenesis. Here we tested the hypothesis that contact of Giardia lamblia with intestinal epithelial cells might lead to release of specific proteins. Using established co-culture models, intestinal ligated loops and a proteomics approach, we identified three G. lamblia proteins (arginine deiminase, ornithine carbamoyl transferase and enolase), previously recognized as immunodominant antigens during acute giardiasis. Release was stimulated by cell-cell interactions, since only small amounts of arginine deiminase and enolase were detected in the medium after culturing of G. lamblia alone. The secreted G. lamblia proteins were localized to the cytoplasm and the inside of the plasma membrane of trophozoites. Furthermore, in vitro studies with recombinant arginine deiminase showed that the secreted Giardia proteins can disable host innate immune factors such as nitric oxide production. These results indicate that contact of Giardia with epithelial cells triggers metabolic enzyme release, which might facilitate effective colonization of the human small intestine.
Authors:
Emma Ringqvist; J E Daniel Palm; Hanna Skarin; Adrian B Hehl; Malin Weiland; Barbara J Davids; David S Reiner; William J Griffiths; Lars Eckmann; Frances D Gillin; Staffan G Svärd
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2008-02-15
Journal Detail:
Title:  Molecular and biochemical parasitology     Volume:  159     ISSN:  0166-6851     ISO Abbreviation:  Mol. Biochem. Parasitol.     Publication Date:  2008 Jun 
Date Detail:
Created Date:  2008-04-28     Completed Date:  2008-07-24     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  8006324     Medline TA:  Mol Biochem Parasitol     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  85-91     Citation Subset:  IM    
Affiliation:
Department of Cell and Molecular Biology, BMC, Uppsala University, Uppsala, Sweden.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Line
Cell Membrane / enzymology
Coculture Techniques
Cytoplasm / enzymology
Electrophoresis, Gel, Two-Dimensional
Epithelial Cells / parasitology*
Giardia lamblia / enzymology*,  immunology
Humans
Hydrolases / isolation & purification,  metabolism
Nitric Oxide / antagonists & inhibitors
Ornithine Carbamoyltransferase / isolation & purification,  metabolism
Phosphopyruvate Hydratase / isolation & purification,  metabolism
Proteomics
Protozoan Proteins / isolation & purification*,  metabolism*
Trophozoites / enzymology
Grant Support
ID/Acronym/Agency:
AI 051687/AI/NIAID NIH HHS; AI 42488/AI/NIAID NIH HHS; DK 35108/DK/NIDDK NIH HHS; GM 61896-04/GM/NIGMS NIH HHS; K26 RR017030/RR/NCRR NIH HHS; P01 DK035108/DK/NIDDK NIH HHS; RR 17030/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/Protozoan Proteins; 10102-43-9/Nitric Oxide; EC 2.1.3.3/Ornithine Carbamoyltransferase; EC 3.-/Hydrolases; EC 3.5.3.6/arginine deiminase; EC 4.2.1.11/Phosphopyruvate Hydratase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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