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Article: A proteomic approach for the identification of bismuth-binding proteins in Helicobacter pylori

TitleA proteomic approach for the identification of bismuth-binding proteins in Helicobacter pylori
Authors
KeywordsColloidal bismuth subcitrate
Helicobacter pylori
Immobilized-metal affinity chromatography
Proteomics
Reactive oxygen species
Issue Date2007
PublisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htm
Citation
Journal of Biological Inorganic Chemistry, 2007, v. 12 n. 6, p. 831-842 How to Cite?
AbstractHelicobacter pylori is a major human pathogen that can cause peptic ulcers and chronic gastritis. Bismuth-based triple or quadruple therapies are commonly recommended for the treatment of H. pylori infections. However, the molecular mechanisms underlying treatment with bismuth are currently not fully understood. We have conducted a detailed comparative proteomic analysis of H. pylori cells both before and after treatment with colloidal bismuth subcitrate (CBS). Eight proteins were found to be significantly upregulated or downregulated in the presence of CBS (20 μg mL -1). Bismuth-induced oxidative stress was confirmed by detecting higher levels of lipid hydroperoxide (approximately 1.8 times) and hemin (approximately 3.4 times), in whole cell extracts of bismuth-treated H. pylori cells, compared with those from untreated cells. The presence of bismuth also led to an approximately eightfold decrease in cellular protease activities. Using immobilized-bismuth affinity chromatography, we isolated and subsequently identified seven bismuth-binding proteins from H. pylori cell extracts. The intracellular levels of four of these proteins (HspA, HspB, NapA and TsaA) were influenced by the addition of CBS, which strongly suggests that they interact directly with bismuth. The other bismuth-interacting proteins identified were two enzymes (fumarase and the urease subunit UreB), and a translational factor (Ef-Tu). Our data suggest that the inhibition of proteases, modulation of cellular oxidative stress and interference with nickel homeostasis may be key processes underlying the molecular mechanism of bismuth's actions against H. pylori. © 2007 SBIC.
Persistent Identifierhttp://hdl.handle.net/10722/77087
ISSN
2015 Impact Factor: 2.495
2015 SCImago Journal Rankings: 0.882
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorGe, Ren_HK
dc.contributor.authorSun, Xen_HK
dc.contributor.authorGu, Qen_HK
dc.contributor.authorWatt, RMen_HK
dc.contributor.authorTanner, JAen_HK
dc.contributor.authorWong, BCYen_HK
dc.contributor.authorXia, HHen_HK
dc.contributor.authorHuang, JDen_HK
dc.contributor.authorHe, QYen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2010-09-06T07:28:07Z-
dc.date.available2010-09-06T07:28:07Z-
dc.date.issued2007en_HK
dc.identifier.citationJournal of Biological Inorganic Chemistry, 2007, v. 12 n. 6, p. 831-842en_HK
dc.identifier.issn0949-8257en_HK
dc.identifier.urihttp://hdl.handle.net/10722/77087-
dc.description.abstractHelicobacter pylori is a major human pathogen that can cause peptic ulcers and chronic gastritis. Bismuth-based triple or quadruple therapies are commonly recommended for the treatment of H. pylori infections. However, the molecular mechanisms underlying treatment with bismuth are currently not fully understood. We have conducted a detailed comparative proteomic analysis of H. pylori cells both before and after treatment with colloidal bismuth subcitrate (CBS). Eight proteins were found to be significantly upregulated or downregulated in the presence of CBS (20 μg mL -1). Bismuth-induced oxidative stress was confirmed by detecting higher levels of lipid hydroperoxide (approximately 1.8 times) and hemin (approximately 3.4 times), in whole cell extracts of bismuth-treated H. pylori cells, compared with those from untreated cells. The presence of bismuth also led to an approximately eightfold decrease in cellular protease activities. Using immobilized-bismuth affinity chromatography, we isolated and subsequently identified seven bismuth-binding proteins from H. pylori cell extracts. The intracellular levels of four of these proteins (HspA, HspB, NapA and TsaA) were influenced by the addition of CBS, which strongly suggests that they interact directly with bismuth. The other bismuth-interacting proteins identified were two enzymes (fumarase and the urease subunit UreB), and a translational factor (Ef-Tu). Our data suggest that the inhibition of proteases, modulation of cellular oxidative stress and interference with nickel homeostasis may be key processes underlying the molecular mechanism of bismuth's actions against H. pylori. © 2007 SBIC.en_HK
dc.languageengen_HK
dc.publisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htmen_HK
dc.relation.ispartofJournal of Biological Inorganic Chemistryen_HK
dc.subjectColloidal bismuth subcitrateen_HK
dc.subjectHelicobacter pylorien_HK
dc.subjectImmobilized-metal affinity chromatographyen_HK
dc.subjectProteomicsen_HK
dc.subjectReactive oxygen speciesen_HK
dc.subject.meshBacterial Proteins - drug effects - genetics - metabolismen_HK
dc.subject.meshCell Lineen_HK
dc.subject.meshGene Expression Profiling - methodsen_HK
dc.subject.meshGene Expression Regulation, Bacterial - drug effectsen_HK
dc.subject.meshHelicobacter pylori - chemistry - drug effects - geneticsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMetalloproteins - analysis - geneticsen_HK
dc.subject.meshMicrobial Sensitivity Testsen_HK
dc.subject.meshNickel - metabolismen_HK
dc.subject.meshOrganometallic Compounds - pharmacologyen_HK
dc.subject.meshProtease Inhibitorsen_HK
dc.subject.meshProteomics - methodsen_HK
dc.titleA proteomic approach for the identification of bismuth-binding proteins in Helicobacter pylorien_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0949-8257&volume=12&spage=831&epage=42&date=2007&atitle=A+proteomic+approach+for+the+identification+of+bismuth-binding+proteins+in+Helicobacter+pylorien_HK
dc.identifier.emailWatt, RM:rmwatt@hku.hken_HK
dc.identifier.emailTanner, JA:jatanner@hku.hken_HK
dc.identifier.emailWong, BCY:bcywong@hku.hken_HK
dc.identifier.emailHuang, JD:jdhuang@hkucc.hku.hken_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authorityWatt, RM=rp00043en_HK
dc.identifier.authorityTanner, JA=rp00495en_HK
dc.identifier.authorityWong, BCY=rp00429en_HK
dc.identifier.authorityHuang, JD=rp00451en_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s00775-007-0237-7en_HK
dc.identifier.pmid17503094-
dc.identifier.scopuseid_2-s2.0-34547404155en_HK
dc.identifier.hkuros131431en_HK
dc.identifier.hkuros128580-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34547404155&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume12en_HK
dc.identifier.issue6en_HK
dc.identifier.spage831en_HK
dc.identifier.epage842en_HK
dc.identifier.isiWOS:000248414100011-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridGe, R=7005525090en_HK
dc.identifier.scopusauthoridSun, X=8906547400en_HK
dc.identifier.scopusauthoridGu, Q=24469982400en_HK
dc.identifier.scopusauthoridWatt, RM=7102907536en_HK
dc.identifier.scopusauthoridTanner, JA=35513993000en_HK
dc.identifier.scopusauthoridWong, BCY=7402023340en_HK
dc.identifier.scopusauthoridXia, HH=35081494200en_HK
dc.identifier.scopusauthoridHuang, JD=8108660600en_HK
dc.identifier.scopusauthoridHe, QY=34770287900en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.citeulike1681659-

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