Bacterial UDP-glucose hydrolases and P2 receptor-mediated responses to infection: A commentary
Abstract
UDP-glucose hydrolases are a group of relatively little known membrane-bound or periplasmic enzymes found in Sal-monella enterica and E. coli. UDP-glucose is an agonist for a specific P2 receptor (P2Y14) found on epithelial cells and cells associated with innate immunity. It is also recognised as a 'danger signal'. Cells respond to mechanical damage by releasing UDP-glucose which activates P2Y14 to trigger an innate immune response; it is postulated that a similar re-sponse to bacterial infection may be protective against infection. However, the UDP-glucose hydrolases may constitute virulence factors able to abrogate this ...
View more >UDP-glucose hydrolases are a group of relatively little known membrane-bound or periplasmic enzymes found in Sal-monella enterica and E. coli. UDP-glucose is an agonist for a specific P2 receptor (P2Y14) found on epithelial cells and cells associated with innate immunity. It is also recognised as a 'danger signal'. Cells respond to mechanical damage by releasing UDP-glucose which activates P2Y14 to trigger an innate immune response; it is postulated that a similar re-sponse to bacterial infection may be protective against infection. However, the UDP-glucose hydrolases may constitute virulence factors able to abrogate this response by degradation of the released UDP-glucose.
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View more >UDP-glucose hydrolases are a group of relatively little known membrane-bound or periplasmic enzymes found in Sal-monella enterica and E. coli. UDP-glucose is an agonist for a specific P2 receptor (P2Y14) found on epithelial cells and cells associated with innate immunity. It is also recognised as a 'danger signal'. Cells respond to mechanical damage by releasing UDP-glucose which activates P2Y14 to trigger an innate immune response; it is postulated that a similar re-sponse to bacterial infection may be protective against infection. However, the UDP-glucose hydrolases may constitute virulence factors able to abrogate this response by degradation of the released UDP-glucose.
View less >
Journal Title
Advances in Infectious Diseases
Volume
3
Issue
2
Copyright Statement
© 2013 The authors and SciRes. This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported (CC BY 3.0) License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Subject
Infectious Diseases