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Article: Surface properties of Helicobacter pylori urease complex are essential for persistence

TitleSurface properties of Helicobacter pylori urease complex are essential for persistence
Authors
Issue Date2010
PublisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.action
Citation
PLoS One, 2010, v. 5 n. 11 How to Cite?
AbstractThe 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. © 2010 Schoep et al.
Persistent Identifierhttp://hdl.handle.net/10722/168492
ISSN
2015 Impact Factor: 3.057
2015 SCImago Journal Rankings: 1.395
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSchoep, TDen_US
dc.contributor.authorFulurija, Aen_US
dc.contributor.authorGood, Fen_US
dc.contributor.authorLu, Wen_US
dc.contributor.authorHimbeck, RPen_US
dc.contributor.authorSchwan, Cen_US
dc.contributor.authorChoi, SSen_US
dc.contributor.authorBerg, DEen_US
dc.contributor.authorMittl, PREen_US
dc.contributor.authorBenghezal, Men_US
dc.contributor.authorMarshall, BJen_US
dc.date.accessioned2012-10-08T03:19:36Z-
dc.date.available2012-10-08T03:19:36Z-
dc.date.issued2010en_US
dc.identifier.citationPLoS One, 2010, v. 5 n. 11en_US
dc.identifier.issn1932-6203en_US
dc.identifier.urihttp://hdl.handle.net/10722/168492-
dc.description.abstractThe 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. © 2010 Schoep et al.en_US
dc.languageengen_US
dc.publisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.actionen_US
dc.relation.ispartofPLoS ONEen_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleSurface properties of Helicobacter pylori urease complex are essential for persistenceen_US
dc.typeArticleen_US
dc.identifier.emailLu, W:luwei@hku.hken_US
dc.identifier.authorityLu, W=rp00754en_US
dc.description.naturepublished_or_final_versionen_US
dc.identifier.doi10.1371/journal.pone.0015042en_US
dc.identifier.pmid21124783-
dc.identifier.scopuseid_2-s2.0-78649735755en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78649735755&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume5en_US
dc.identifier.issue11en_US
dc.identifier.isiWOS:000284686500022-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridSchoep, TD=22235557000en_US
dc.identifier.scopusauthoridFulurija, A=6602613332en_US
dc.identifier.scopusauthoridGood, F=36997896300en_US
dc.identifier.scopusauthoridLu, W=27868087600en_US
dc.identifier.scopusauthoridHimbeck, RP=6506300992en_US
dc.identifier.scopusauthoridSchwan, C=36998081100en_US
dc.identifier.scopusauthoridChoi, SS=15031343000en_US
dc.identifier.scopusauthoridBerg, DE=7202401139en_US
dc.identifier.scopusauthoridMittl, PRE=6701704224en_US
dc.identifier.scopusauthoridBenghezal, M=6603042586en_US
dc.identifier.scopusauthoridMarshall, BJ=7202280032en_US

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