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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-43093

Schoep, T D; Fulurija, A; Good, F; Lu, W; Himbeck, R P; Schwan, C; Choi, S S; Berg, D E; Mittl, P R E; Benghezal, M; Marshall, B J (2010). Surface properties of Helicobacter pylori urease complex are essential for persistence. PLoS ONE, 5(11):e15042.

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Creative Commons: Attribution 4.0 International (CC BY 4.0)
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The enzymatic activity of Helicobacter pylori's urease neutralises stomach acidity, thereby promoting infection by this pathogen. Urease protein has also been found to interact with host cells in vitro, although this property's possible functional importance has not been studied in vivo. To test for a role of the urease surface in the host/pathogen interaction, surface exposed loops that display high thermal mobility were targeted for inframe insertion mutagenesis. H. pylori expressing urease with insertions at four of eight sites tested retained urease activity, which in three cases was at least as stable as was wild-type urease at pH 3. Bacteria expressing one of these four mutant ureases, however, failed to colonise mice for even two weeks, and a second had reduced bacterial titres after longer term (3 to 6 months) colonisation. These results indicate that a discrete surface of the urease complex is important for H. pylori persistence during gastric colonisation. We propose that this surface interacts directly with host components important for the host-pathogen interaction, immune modulation or other actions that underlie H. pylori persistence in its special gastric mucosal niche.


11 citations in Web of Science®
10 citations in Scopus®
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63 downloads since deposited on 26 Jan 2011
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Deposited On:26 Jan 2011 16:37
Last Modified:05 Jul 2016 11:42
Publisher:Public Library of Science (PLoS)
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1371/journal.pone.0015042
PubMed ID:21124783

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