ArticleRedox biology2019
Quantifying changes in the bacterial thiol redox proteome during host-pathogen interaction.
Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
- Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024Review
- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- Dual RNA-Seq ofPathogens (Basel, Switzerland) · 2023Article
- Evidence that protein thiols are not primary targets of intracellular reactive oxygen species in growingFrontiers in microbiology · 2023Article
- Article
- Article
- Mass Spectrometry-Based Quantitative Cysteine Redox Proteome Profiling of Isolated Mitochondria Using Differential iodoTMT Labeling.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Redox proteomic study of Bacillus cereus thiol proteome during fermentative anaerobic growth.BMC genomics · 2021Article
- Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.Antioxidants (Basel, Switzerland) · 2021Review
- New Provisional Function of OmpA frommSystems · 2021Article
- The Redox Proteome of Thiol Proteins in the Rice Blast FungusFrontiers in microbiology · 2021Article
- The effects of neutrophil-generated hypochlorous acid and other hypohalous acids on host and pathogens.Cellular and molecular life sciences : CMLS · 2021Review
- Chemical tools for decoding redox signaling at the host-microbe interface.PLoS pathogens · 2020Article
- Regulation of titin-based cardiac stiffness by unfolded domain oxidation (UnDOx).Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Bacterial Defense Systems against the Neutrophilic Oxidant Hypochlorous Acid.Infection and immunity · 2020Review
- The minimal meningococcal ProQ protein has an intrinsic capacity for structure-based global RNA recognition.Nature communications · 2020Article
- Activation leads to a significant shift in the intracellular redox homeostasis of neutrophil-like cells.Redox biology · 2020Article
- Exposure ofThe Journal of biological chemistry · 2019Article
- Stress-induced chaperones: a first line of defense against the powerful oxidant hypochlorous acid.F1000Research · 2019Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phagocyte-derived production of a complex mixture of different oxidants is a major mechanism of the host defense against microbial intruders. On the protein level, a major target of these oxidants is the thiol group of the amino acid cysteine in proteins. Oxidation of thiol groups is a widespread regulatory post-translational protein modification. It is used by bacteria to respond to and to overcome oxidative stress. Numerous redox proteomic studies have shown that protein thiols in bacteria, such as Escherichia coli react towards a number of oxidants in specific ways. However, our knowledge about protein thiols in bacteria exposed to the complex mixture of oxidants encountered in the phagolysosome is still limited. In this study, we used a quantitative redox proteomic method (OxICAT) to assess the in vivo thiol oxidation status of phagocytized E. coli. The majority (65.5%) of identified proteins harbored thiols that were significantly oxidized (> 30%) upon phagocytosis. A substantial number of these proteins are from major metabolic pathways or are involved in cell detoxification and stress response, suggesting a systemic breakdown of the bacterial cysteine proteome in phagocytized bacteria. 16 of the oxidized proteins provide E. coli with a significant growth advantage in the presence of H
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