ArticleThe Journal of biological chemistry2011
Synergistic roles of Helicobacter pylori methionine sulfoxide reductase and GroEL in repairing oxidant-damaged catalase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.
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Who cites it
34 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.
- Infiltration to infection: key virulence players of Helicobacter pylori pathogenicity.Infection · 2024Pooled it
- Molecular characterization of H. pylori: genetic diversity and vacA s1m1/cagA+ prevalence in Western Algeria.Molecular genetics and genomics : MGG · 2026Article
- An integrated Msr-antioxidase-host gene circuit maintains redox homeostasis in legume-rhizobium symbiosis.Frontiers in plant science · 2026Article
- Pan msr gene deleted strain of Salmonella Typhimurium suffers oxidative stress, depicts macromolecular damage and attenuated virulence.Scientific reports · 2023Article
- Periplasmic methionine sulfoxide reductase (MsrP)-a secondary factor in stress survival and virulence of Salmonella Typhimurium.FEMS microbiology letters · 2023Article
- Positive Selection of Mutations in the Helicobacter pyloriInfection and immunity · 2022Article
- FromWorld journal of clinical oncology · 2022Review
- HP1021 is a redox switch protein identified in Helicobacter pylori.Nucleic acids research · 2021Article
- Methionine Sulfoxide Reductases Contribute to Anaerobic Fermentative Metabolism inAntioxidants (Basel, Switzerland) · 2021Article
- Methionine Redox Homeostasis in Protein Quality Control.Frontiers in molecular biosciences · 2021Review
- Review
- Identification of oxidant susceptible proteins in Salmonella Typhimurium.Molecular biology reports · 2020Article
- Loss of methionine sulfoxide reductases increases resistance to oxidative stress.Free radical biology & medicine · 2019Article
- Helicobacter pylori senses bleach (HOCl) as a chemoattractant using a cytosolic chemoreceptor.PLoS biology · 2019Article
- Drosophila methionine sulfoxide reductase A (MSRA) lacks methionine oxidase activity.Free radical biology & medicine · 2019Article
- Methionine in Proteins: It's Not Just for Protein Initiation Anymore.Neurochemical research · 2019Review
- The Role of Methionine Sulfoxide Reductases in Oxidative Stress Tolerance and Virulence ofAntioxidants (Basel, Switzerland) · 2018Review
- Reduce, Induce, Thrive: Bacterial Redox Sensing during Pathogenesis.Journal of bacteriology · 2018Review
- Noncatalytic Antioxidant Role for Helicobacter pylori Urease.Journal of bacteriology · 2018Article
- Myristoylated methionine sulfoxide reductase A is a late endosomal protein.The Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Hypochlorous acid (HOCl) produced via the enzyme myeloperoxidase is a major antibacterial oxidant produced by neutrophils, and Met residues are considered primary amino acid targets of HOCl damage via conversion to Met sulfoxide. Met sulfoxide can be repaired back to Met by methionine sulfoxide reductase (Msr). Catalase is an important antioxidant enzyme; we show it constitutes 4-5% of the total Helicobacter pylori protein levels. msr and katA strains were about 14- and 4-fold, respectively, more susceptible than the parent to killing by the neutrophil cell line HL-60 cells. Catalase activity of an msr strain was much more reduced by HOCl exposure than for the parental strain. Treatment of pure catalase with HOCl caused oxidation of specific MS-identified Met residues, as well as structural changes and activity loss depending on the oxidant dose. Treatment of catalase with HOCl at a level to limit structural perturbation (at a catalase/HOCl molar ratio of 1:60) resulted in oxidation of six identified Met residues. Msr repaired these residues in an in vitro reconstituted system, but no enzyme activity could be recovered. However, addition of GroEL to the Msr repair mixture significantly enhanced catalase activity recovery. Neutrophils produce large amounts of HOCl at inflammation sites, and bacterial catalase may be a prime target of the host inflammatory response; at high concentrations of HOCl (1:100), we observed loss of catalase secondary structure, oligomerization, and carbonylation. The same HOCl-sensitive Met residue oxidation targets in catalase were detected using chloramine-T as a milder oxidant.
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Registered trials
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