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Article: Urease inactivation by an unusual GroES chaperonin

TitleUrease inactivation by an unusual GroES chaperonin
Authors
Cun, SJSun, H
KeywordsGroES chaperonin
Helicobacter pylori
metal binding
microbial pathogenesis
nickel
urease inactivation
Issue Date2014
PublisherScience China Press, co-published with Springer. The Journal's web site is located at http://chem.scichina.com:8081/sciBe/EN/volumn/current.shtml
Citation
Science China Chemistry, 2014, v. 57 n. 6, p. 842-848 How to Cite?
DOI: http://dx.doi.org/10.1007/s11426-014-5088-9
AbstractIt remains uncovered yet how the common gastric pathogen, Helicobacter pylori, survives through the acidic barrier and the immune response simultaneously in the stomach. Herein we report a unique GroES chaperonin that effectively inactivates Helicobacter pylori urease in Escherichia coli model. Such a function depends on the quaternary structure as well as the metal binding at the C terminus. Surprisingly, the C-terminal metal capacity seems not closely relevant to the apparent urease inactivation. Our findings have possibly revealed a survival strategy of Helicobacter pylori after its gastric localization. © 2014 Science China Press and Springer-Verlag Berlin Heidelberg.
Persistent Identifierhttp://hdl.handle.net/10722/202608
ISSN
1674-7291
2023 Impact Factor: 10.4
2023 SCImago Journal Rankings: 2.316
ISI Accession Number ID
WOS:000336747700007

 

DC FieldValueLanguage
dc.contributor.authorCun, SJ-
dc.contributor.authorSun, H-
dc.date.accessioned2014-09-19T08:42:29Z-
dc.date.available2014-09-19T08:42:29Z-
dc.date.issued2014-
dc.identifier.citationScience China Chemistry, 2014, v. 57 n. 6, p. 842-848-
dc.identifier.issn1674-7291-
dc.identifier.urihttp://hdl.handle.net/10722/202608-
dc.description.abstractIt remains uncovered yet how the common gastric pathogen, Helicobacter pylori, survives through the acidic barrier and the immune response simultaneously in the stomach. Herein we report a unique GroES chaperonin that effectively inactivates Helicobacter pylori urease in Escherichia coli model. Such a function depends on the quaternary structure as well as the metal binding at the C terminus. Surprisingly, the C-terminal metal capacity seems not closely relevant to the apparent urease inactivation. Our findings have possibly revealed a survival strategy of Helicobacter pylori after its gastric localization. © 2014 Science China Press and Springer-Verlag Berlin Heidelberg.-
dc.languageeng-
dc.publisherScience China Press, co-published with Springer. The Journal's web site is located at http://chem.scichina.com:8081/sciBe/EN/volumn/current.shtml-
dc.relation.ispartofScience China Chemistry-
dc.rightsThe original publication is available at www.scichina.com and www.springerlink.com-
dc.subjectGroES chaperonin-
dc.subjectHelicobacter pylori-
dc.subjectmetal binding-
dc.subjectmicrobial pathogenesis-
dc.subjectnickel-
dc.subjecturease inactivation-
dc.titleUrease inactivation by an unusual GroES chaperonin-
dc.typeArticle-
dc.identifier.emailSun, H: hsun@hku.hk-
dc.identifier.authoritySun, H=rp00777-
dc.identifier.doi10.1007/s11426-014-5088-9-
dc.identifier.scopuseid_2-s2.0-84902266824-
dc.identifier.hkuros239334-
dc.identifier.volume57-
dc.identifier.issue6-
dc.identifier.spage842-
dc.identifier.epage848-
dc.identifier.isiWOS:000336747700007-
dc.publisher.placeChina-
dc.identifier.issnl1869-1870-

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