ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2007
A proteomic approach for the identification of bismuth-binding proteins in Helicobacter pylori.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 101 citations in OpenAlex.
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- Selective inhibition of NikA mediated Ni(II) import in E. coli by the Indium(III)-EDTA complex.Metallomics : integrated biometal science · 2025Article
- New insights into iron uptake in Streptococcus mutans: evidence for a role of siderophore-like molecules.Archives of microbiology · 2025Article
- In Vitro Susceptibility and Synergistic Effect of Bismuth AgainstAntibiotics (Basel, Switzerland) · 2024Article
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- Flavodoxins as Novel Therapeutic Targets againstInternational journal of molecular sciences · 2020Review
- Multi-omics and temporal dynamics profiling reveal disruption of central metabolism inChemical science · 2018Article
- Metallochaperone UreG serves as a new target for design of urease inhibitor: A novel strategy for development of antimicrobials.PLoS biology · 2018Article
- Functional disruption of peroxiredoxin by bismuth antiulcer drugs attenuates Helicobacter pylori survival.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Integrative approach for the analysis of the proteome-wide response to bismuth drugs inChemical science · 2017Article
- Microbial Metalloproteomics.Proteomes · 2015Review
- The impact of bismuth addition to sequential treatment on Helicobacter pylori eradication: A pilot study.Bosnian journal of basic medical sciences · 2015Article
- Colloidal bismuth subcitrate impedes proton entry into Helicobacter pylori and increases the efficacy of growth-dependent antibiotics.Alimentary pharmacology & therapeutics · 2015Article
- Glutathione and multidrug resistance protein transporter mediate a self-propelled disposal of bismuth in human cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Current and potential applications of bismuth-based drugs.Molecules (Basel, Switzerland) · 2014Review
- Metal-based drugs.Science progress · 2014Review
- Crystal structure, antibacterial and cytotoxic activities of a new complex of bismuth(III) with sulfapyridine.Molecules (Basel, Switzerland) · 2013Article
- Recent advances in bioinorganic chemistry of bismuth.Current opinion in chemical biology · 2012Review
- A proteomic approach to identification of plutonium-binding proteins in mammalian cells.Journal of proteomics · 2012Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Helicobacter 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 microg 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.
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