Document Detail


An NSP4-dependant mechanism by which rotavirus impairs lactase enzymatic activity in brush border of human enterocyte-like Caco-2 cells.
MedLine Citation:
PMID:  17506819     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Lactase-phlorizin hydrolase (LPH, EC 3.2.1.23-62) is a brush border membrane (BBM)-associated enzyme in intestinal cells that hydrolyse lactose, the most important sugar in milk. Impairing in lactase activity during rotavirus infection has been described in diseased infants but the mechanism by which the functional lesion occurs remains unknown. We undertook a study to elucidate whether rotavirus impairs the lactase enzymatic activity in BBM of human enterocyte cells. In this study we use cultured human intestinal fully differentiated enterocyte-like Caco-2 cells to demonstrate how the lactase enzymatic activity at BBM is significantly decreased in rhesus monkey rotavirus (RRV)-infected cells. We found that the decrease in enzyme activity is not dependent of the Ca(2+)- and cAMP-dependent signalling events triggered by the virus. The LPH biosynthesis, stability, and expression of the protein at the BBM of infected cells were not modified. We provide evidence that in RRV-infected cells the kinetic of lactase enzymatic activity present at the BBM was modified. Both BBM(control) and BBM(RRV) have identical K(m) values, but hydrolyse the substrate at different rates. Thus, the BBM(RRV) exhibits almost a 1.5-fold decreased V(max) than that of BBM(control) and is therefore enzymatically less active than the latter. Our study demonstrate conclusively that the impairment of lactase enzymatic activity at the BBM of the enterocyte-like Caco-2 cells observed during rotavirus infection results from an inhibitory action of the secreted non-structural rotavirus protein NSP4.
Authors:
Isabelle Beau; Jacqueline Cotte-Laffitte; Monique Géniteau-Legendre; Mary K Estes; Alain L Servin
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2007-05-15
Journal Detail:
Title:  Cellular microbiology     Volume:  9     ISSN:  1462-5814     ISO Abbreviation:  Cell. Microbiol.     Publication Date:  2007 Sep 
Date Detail:
Created Date:  2007-08-16     Completed Date:  2008-04-28     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100883691     Medline TA:  Cell Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  2254-66     Citation Subset:  IM    
Affiliation:
INSERM, UMR 756, Signalisation et Physiopathologie des Cellules Epithéliales, Châtenay-Malabry, France.
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MeSH Terms
Descriptor/Qualifier:
Animals
Antigens, Viral / genetics,  metabolism*
Caco-2 Cells / cytology,  enzymology*,  microbiology
Glycoproteins / genetics,  metabolism*
Glycosylceramidase / metabolism*
Humans
Microvilli / enzymology*,  microbiology
Receptors, Virus / genetics,  metabolism
Rotavirus / metabolism*
Rotavirus Infections / enzymology
Toxins, Biological / genetics,  metabolism*
Viral Nonstructural Proteins / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
DK30144/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Antigens, Viral; 0/Glycoproteins; 0/NS28 protein, rotavirus; 0/Receptors, Virus; 0/Toxins, Biological; 0/Viral Nonstructural Proteins; EC 3.2.1.62/Glycosylceramidase

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


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