Cited by 177Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressSalmonella and Campylobacter epidemiology

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Disparate Impact of Oxidative Host Defenses Determines the Fate of Salmonella during Systemic Infection in Mice

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Burton, Neil A., Schürmann, Nura, Casse, Olivier, Steeb, Anne K., Claudi, Beatrice, Zankl, Janine, Schmidt, Alexander, Bumann, Dirk·2014·Cell Host & Microbe

DOI 10.1016/j.chom.2013.12.006

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Abstract

Reactive oxygen and nitrogen species function in host defense via mechanisms that remain controversial. Pathogens might encounter varying levels of these species, but bulk measurements cannot resolve such heterogeneity. We used single-cell approaches to determine the impact of oxidative and nitrosative stresses on individual Salmonella during early infection in mouse spleen. Salmonella encounter and respond to both stresses, but the levels and impact vary widely. Neutrophils and inflammatory monocytes kill Salmonella by generating overwhelming oxidative stress through NADPH oxidase and myeloperoxidase. This controls Salmonella within inflammatory lesions but does not prevent their spread to more permissive resident red pulp macrophages, which generate only sublethal oxidative bursts. Regional host expression of inducible nitric oxide synthase exposes some Salmonella to nitrosative stress, triggering effective local Salmonella detoxification through nitric oxide denitrosylase. Thus, reactive oxygen and nitrogen species influence dramatically different outcomes of disparate Salmonella-host cell encounters, which together determine overall disease progression.

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One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products.
Datsenko, K., & Wanner, B. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.120163297 · Cited by 15,902
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Aromatic-dependent Salmonella typhimurium are non-virulent and effective as live vaccines
Hoiseth, S. K., & Stocker, B. A. D. (1981) · Nature · doi:10.1038/291238a0 · Cited by 2,088
Antimicrobial reactive oxygen and nitrogen species: concepts and controversies
Fang, F. C. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1004 · Cited by 1,676
Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
Nathan, C., & Shiloh, M. U. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.8841 · Cited by 1,469
Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
Miao, E. A., Leaf, I. A., Treuting, P. M., Mao, D. P., Dors, M., Sarkar, A., Warren, S. E., Wewers, M. D., & Aderem, A. (2010) · Nature Immunology · doi:10.1038/ni.1960 · Cited by 1,336
Use of Ly6G-specific monoclonal antibody to deplete neutrophils in mice
Daley, J. M., Thomay, A. A., Connolly, M. D., Reichner, J. S., & Albina, J. E. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0407247 · Cited by 1,047
Revisiting the role of the granuloma in tuberculosis
Ramakrishnan, L. (2012) · Nature reviews. Immunology · doi:10.1038/nri3211 · Cited by 943
Myeloperoxidase: a front-line defender against phagocytosed microorganisms
Klebanoff, S. J., Kettle, A. J., Rosen, H., Winterbourn, C. C., & Nauseef, W. M. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0712349 · Cited by 679
Modeling the Reactions of Superoxide and Myeloperoxidase in the Neutrophil Phagosome
Winterbourn, C. C., Hampton, M. B., Livesey, J. H., & Kettle, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605898200 · Cited by 633
Salmonella Pathogenicity Island 2-Dependent Evasion of the Phagocyte NADPH Oxidase
Vázquez‐Torres, A., Xu, Y., Jones‐Carson, J., Holden, D. W., Lucia, S. M., Dinauer, M. C., Mastroeni, P., & Fang, F. C. (2000) · Science · doi:10.1126/science.287.5458.1655 · Cited by 557
Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1
Broz, P., Ruby, T., Belhocine, K., Bouley, D. M., Kayagaki, N., Dixit, V. M., & Monack, D. M. (2012) · Nature · doi:10.1038/nature11419 · Cited by 535
Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. I. Effects on microbial killing by activated peritoneal macrophages in vitro
Vazquez-Torres, A., Jones-Carson, J., Mastroeni, P., Ischiropoulos, H., & Fang, F. C. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.2.227 · Cited by 530
A Palette of Fluorescent Probes with Varying Emission Colors for Imaging Hydrogen Peroxide Signaling in Living Cells
Dickinson, B. C., Huynh, C., & Chang, C. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1014103 · Cited by 520
Murine Salmonellosis Studied by Confocal Microscopy: Salmonella typhimurium Resides Intracellularly Inside Macrophages and Exerts a Cytotoxic Effect on Phagocytes In Vivo
Richter-Dahlfors, A., Buchan, A. M. J., & Finlay, B. B. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.4.569 · Cited by 502
Hydrogen Peroxide Fluxes and Compartmentalization inside Growing Escherichia coli
Seaver, L. C., & Imlay, J. A. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.24.7182-7189.2001 · Cited by 456
How does the oxidative burst of macrophages kill bacteria? Still an open question
Slauch, J. M. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07612.x · Cited by 436
Self-destructive cooperation mediated by phenotypic noise
Ackermann, M., Stecher, B., Freed, N. E., Songhet, P., Hardt, W., & Doebeli, M. (2008) · Nature · doi:10.1038/nature07067 · Cited by 432
Antimicrobial Actions of the Nadph Phagocyte Oxidase and Inducible Nitric Oxide Synthase in Experimental Salmonellosis. II. Effects on Microbial Proliferation and Host Survival in Vivo
Mastroeni, P., Vazquez-Torres, A., Fang, F. C., Xu, Y., Khan, S., Hormaeche, C. E., & Dougan, G. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.2.237 · Cited by 399
Antimicrobial Actions of Reactive Oxygen Species
Fang, F. C. (2011) · mBio · doi:10.1128/mbio.00141-11 · Cited by 387
Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase
Groote, M. A. D., Ochsner, U. A., Shiloh, M. U., Nathan, C., McCord, J. M., Dinauer, M. C., Libby, S. J., Vázquez‐Torres, A., Xu, Y., & Fang, F. C. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.25.13997 · Cited by 386
Salmonella Pathogenicity Island 2 Mediates Protection of Intracellular Salmonella from Reactive Nitrogen Intermediates
Chakravortty, D., Hansen-Wester, I., & Hensel, M. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20011547 · Cited by 344
Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx - mutants of Escherichia coli
Park, S., You, X., & Imlay, J. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502051102 · Cited by 342
Stabilization of cooperative virulence by the expression of an avirulent phenotype
Diard, M., García, V., Maier, L., Remus‐Emsermann, M. N. P., Regoes, R. R., Ackermann, M., & Hardt, W. (2013) · Nature · doi:10.1038/nature11913 · Cited by 324
Dynamics of intracellular bacterial replication at the single cell level
Hélaine, S., Thompson, J. A., Watson, K. G., Liu, M., Boyle, C., & Holden, D. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000041107 · Cited by 319
Flavorubredoxin, an Inducible Catalyst for Nitric Oxide Reduction and Detoxification in Escherichia coli
Gardner, A. M., Helmick, R. A., & Gardner, P. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110471200 · Cited by 314
Neutrophils Exert Protection in the Early Tuberculous Granuloma by Oxidative Killing of Mycobacteria Phagocytosed from Infected Macrophages
Yang, C.-T., Cambier, C. J., Davis, J. M., Hall, C. J., Crosier, P. S., & Ramakrishnan, L. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.07.009 · Cited by 293
Modelling within-Host Spatiotemporal Dynamics of Invasive Bacterial Disease
Grant, A. J., Restif, O., McKinley, T. J., Sheppard, M., Maskell, D. J., & Mastroeni, P. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060074 · Cited by 260
Nitric oxide potentiates hydrogen peroxide-induced killing of Escherichia coli.
Pacelli, R., Wink, D. A., Cook, J. A., Krishna, M. C., DeGraff, W., Friedman, N., Tsokos, M., Samuni, A., & Mitchell, J. B. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.5.1469 · Cited by 260
Critical roles of neutrophils in host defense against experimental systemic infections of mice by Listeria monocytogenes, Salmonella typhimurium, and Yersinia enterocolitica
Conlan, J. W. (1997) · Infection and Immunity · doi:10.1128/iai.65.2.630-635.1997 · Cited by 208
Peroxide-Sensing Transcriptional Regulators in Bacteria
Dubbs, J. M., & Mongkolsuk, S. (2012) · Journal of Bacteriology · doi:10.1128/jb.00304-12 · Cited by 207
Human macrophage host defense against Mycobacterium tuberculosis
Liu, P. T., & Modlin, R. L. (2008) · Current Opinion in Immunology · doi:10.1016/j.coi.2008.05.014 · Cited by 202
Maintenance of Nitric Oxide and Redox Homeostasis by the Salmonella Flavohemoglobin Hmp
Bang, I. S., Liu, L., Vázquez‐Torres, A., Crouch, M. V., Stamler, J. S., & Fang, F. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605174200 · Cited by 189
Parallel Exploitation of Diverse Host Nutrients Enhances Salmonella Virulence
Steeb, B., Claudi, B., Burton, N. A., Tienz, P., Schmidt, A., Farhan, H., Mazé, A., & Bumann, D. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003301 · Cited by 181
Self-citation
In vivo, fliC expression by Salmonella enterica serovar Typhimurium is heterogeneous, regulated by ClpX, and anatomically restricted
Cummings, L. A., Wilkerson, W. D., Bergsbaken, T., & Cookson, B. T. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05271.x · Cited by 179
A potential role for periplasmic superoxide dismutase in blocking the penetration of external superoxide into the cytosol of Gram‐negative bacteria
Korshunov, S., & Imlay, J. A. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02719.x · Cited by 178
Balance between Endogenous Superoxide Stress and Antioxidant Defenses
Gort, A. S., & Imlay, J. A. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.6.1402-1410.1998 · Cited by 173
Mycobacterium tuberculosis Responds to Chloride and pH as Synergistic Cues to the Immune Status of its Host Cell
Tan, S., Sukumar, N., Abramovitch, R. B., Parish, T., & Russell, D. G. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003282 · Cited by 164
Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen
Hausladen, A., Gow, A. J., & Stamler, J. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181199698 · Cited by 163
Induction of nitric oxide synthesis and xanthine oxidase and their roles in the antimicrobial mechanism against Salmonella typhimurium infection in mice
Umezawa, K., Akaike, T., Fujii, S., Suga, M., Setoguchi, K., Ozawa, A., & Maeda, H. (1997) · Infection and Immunity · doi:10.1128/iai.65.7.2932-2940.1997 · Cited by 154
The Transcriptional Repressor Protein NsrR Senses Nitric Oxide Directly via a [2Fe-2S] Cluster
Tucker, N. P., Hicks, M. G., Clarke, T. A., Crack, J. C., Chandra, G., Brun, N. E. L., Dixon, R. A., & Hutchings, M. I. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003623 · Cited by 148
Monocyte Recruitment, Activation, and Function in the Gut-Associated Lymphoid Tissue during Oral Salmonella Infection
Rydström, A., & Wick, M. J. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.9.5789 · Cited by 147
Dynamics of bacterial growth and distribution within the liver duringSalmonellainfection
Sheppard, M., Webb, C. R., Heath, F., Mallows, V., Emilianus, R., Maskell, D. J., & Mastroeni, P. (2003) · Cellular Microbiology · doi:10.1046/j.1462-5822.2003.00296.x · Cited by 144
Escherichia coli Di-iron YtfE Protein Is Necessary for the Repair of Stress-damaged Iron-Sulfur Clusters
Justino, M. C., Almeida, C., Teixeira, M. S., & Saraiva, L. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610656200 · Cited by 140
Multiple Targets of Nitric Oxide in the Tricarboxylic Acid Cycle of Salmonella enterica Serovar Typhimurium
Richardson, A. R., Payne, E. C., Younger, N. S., Karlinsey, J. E., Thomas, V. C., Becker, L. A., Navarre, W. W., Castor, M. E., Libby, S. J., & Fang, F. C. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.06.004 · Cited by 134
Reactive Oxygen Species and Nitric Oxide in Cutaneous Leishmaniasis
Horta, M. F., Mendes, B. P., Roma, E. H., Noronha, F. S. M., Macêdo, J. P., de Oliveira, L. S., Duarte, M. M., & Vieira, L. Q. (2012) · Journal of Parasitology Research · doi:10.1155/2012/203818 · Cited by 131
Regulation of host immune responses by modification of Salmonella virulence genes
VanCott, J. L., Chatfield, S. N., Roberts, M., Hone, D. M., Hohmann, E. L., Pascual, D. W., Yamamoto, M., Kiyono, H., & McGhee, J. R. (1998) · Nature Medicine · doi:10.1038/3227 · Cited by 131
Nitric Oxide Homeostasis in Salmonella typhimurium
Gilberthorpe, N. J., & Poole, R. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708019200 · Cited by 130
What really happens in the neutrophil phagosome?
Hurst, J. K. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.008 · Cited by 124
Nitric Oxide and Salmonella Pathogenesis
Henard, C. A., & Vázquez‐Torres, A. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00084 · Cited by 123
A combination of cytochrome c nitrite reductase (NrfA) and flavorubredoxin (NorV) protects Salmonella enterica serovar Typhimurium against killing by NO in anoxic environments
Mills, P. C., Rowley, G., Spiro, S., Hinton, J. C. D., & Richardson, D. J. (2008) · Microbiology · doi:10.1099/mic.0.2007/014290-0 · Cited by 120
Hydroxylamine Reductase Activity of the Hybrid Cluster Protein from Escherichia coli
Wolfe, M. T., Heo, J., Garavelli, J. S., & Ludden, P. W. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.21.5898-5902.2002 · Cited by 110
Salmonella detoxifying enzymes are sufficient to cope with the host oxidative burst
Aussel, L., Zhao, W., Hébrard, M., Guilhon, A., Viala, J. P. M., Henri, S., Chasson, L., Gorvel, J., Barras, F., & Méresse, S. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07611.x · Cited by 107
Hemophagocytic macrophages harbor Salmonella enterica during persistent infection
Nix, R. N., Altschuler, S. E., Henson, P. M., & Detweiler, C. S. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030193 · Cited by 104
The crucial role of polymorphonuclear leukocytes in resistance to Salmonella dublin infections in genetically susceptible and resistant mice
Vassiloyanakopoulos, A. P., Okamoto, S., & Fierer, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7676 · Cited by 103
Phagocytic Superoxide Specifically Damages an Extracytoplasmic Target to Inhibit or Kill Salmonella
Craig, M., & Slauch, J. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004975 · Cited by 99
Antigen selection based on expression levels during infection facilitates vaccine development for an intracellular pathogen
Rollenhagen, C., Soerensen, M., Rizos, K., Hurwitz, R., & Bumann, D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401283101 · Cited by 99
Self-citation
Intraphagosomal Measurement of the Magnitude and Duration of the Oxidative Burst
VanderVen, B. C., Yates, R. M., & Russell, D. G. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00877.x · Cited by 98
Myeloperoxidase-rich Ly-6C+ myeloid cells infiltrate allografts and contribute to an imaging signature of organ rejection in mice
Świrski, F. K., Wildgruber, M., Ueno, T., Figueiredo, J., Panizzi, P. R., Iwamoto, Y., Zhang, E., Stone, J. R., Rodríguez, E., Chen, J. W., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42304 · Cited by 98
NsrR: a key regulator circumventing Salmonella enterica serovar Typhimurium oxidative and nitrosative stress in vitro and in IFN-γ-stimulated J774.2 macrophages
Gilberthorpe, N. J., Lee, M. E., Stevanin, T. M., Read, R. C., & Poole, R. K. (2007) · Microbiology · doi:10.1099/mic.0.2006/003731-0 · Cited by 94
Systemic infection of mice by wild-type but not Spv- Salmonella typhimurium is enhanced by neutralization of gamma interferon and tumor necrosis factor alpha
Gulig, P. A., Doyle, T. J., Clare-Salzler, M. J., Maiese, R. L., & Matsui, H. (1997) · Infection and Immunity · doi:10.1128/iai.65.12.5191-5197.1997 · Cited by 91
Immunity to Intracellular Salmonella Depends on Surface-associated Antigens
Barat, S., Willer, Y., Rizos, K., Claudi, B., Mazé, A., Schemmer, A. K., Kirchhoff, D., Schmidt, A., Burton, N., & Bumann, D. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002966 · Cited by 88
Self-citation
Differential accumulation of Salmonella[Cu, Zn] superoxide dismutases SodCI and SodCII in intracellular bacteria: correlation with their relative contribution to pathogenicity
Uzzau, S., Bossi, L., & Figueroa‐Bossi, N. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03145.x · Cited by 81
The primary effect of the Ity locus is on the rate of growth of Salmonella typhimurium that are relatively protected from killing.
Benjamin, W. H., Hall, P., Roberts, S., & Briles, D. E. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.8.3143 · Cited by 76
The in vivo division and death rates of Salmonella typhimurium in the spleens of naturally resistant and susceptible mice measured by the superinfecting phage technique of Meynell.
Hormaeche, C. E. (1980) · PubMed · Cited by 63
Polyamine-Mediated Resistance of Uropathogenic Escherichia coli to Nitrosative Stress
Bower, J. M., & Mulvey, M. A. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.3.928-933.2006 · Cited by 60
Modulation of Virulence by Two Acidified Nitrite-Responsive Loci ofSalmonella entericaSerovar Typhimurium
Kim, C. C., Monack, D. M., & Falkow, S. (2003) · Infection and Immunity · doi:10.1128/iai.71.6.3196-3205.2003 · Cited by 60
Slc11a1-mediated resistance toSalmonella entericaserovar Typhimurium andLeishmania donovaniinfections does not require functional inducible nitric oxide synthase or phagocyte oxidase activity
White, J. K., Mastroeni, P., Popoff, J.-F., Evans, C. A., & Blackwell, J. M. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0904546 · Cited by 51
Oxidative Stress
Imlay, J. A. (2009) · EcoSal Plus · doi:10.1128/ecosalplus.5.4.4 · Cited by 46
Nitric oxide-sensing mechanisms in Escherichia coli
Spiro, S. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340200 · Cited by 45
Monocyte and neutrophil recruitment during oral Salmonella infection is driven by MyD88‐derived chemokines
Rydström, A., & Wick, M. J. (2009) · European Journal of Immunology · doi:10.1002/eji.200939483 · Cited by 43
Visualisation of Nitric Oxide Generated by Activated Murine Macrophages
Leone, A., Fürst, V., Foxwell, N., Cellek, S., & Moncada, S. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0557 · Cited by 36
A Fluorescently Tagged C-Terminal Fragment of p47phoxDetects NADPH Oxidase Dynamics during Phagocytosis
Li, X. J., Tian, W., Stull, N. D., Grinstein, S., Atkinson, S. J., & Dinauer, M. C. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-06-0620 · Cited by 34
Properties of isolated red pulp macrophages from mouse spleen.
Nusrat, A., Wright, S. D., Aderem, A. A., Steinman, R. M., & Cohn, Z. A. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.168.4.1505 · Cited by 28
Electron microscopic studies on the location of bacterial proliferation in the liver in murine salmonellosis.
Lin, F.-P., Wang, X. M., Hsu, H. S., Mumaw, V. R., & Nakoneczna, I. (1987) · PubMed Central · Cited by 28
Early responses to Salmonella typhimurium infection in mice occur at focal lesions in infected organs
Khan, S. A., Strijbos, P. J. L. M., Everest, P. H., Moss, D., Stratford, R., Mastroeni, P., Allen, J., Servos, S., Charles, I. G., Dougan, G., et al. (2001) · Microbial Pathogenesis · doi:10.1006/mpat.2000.0405 · Cited by 24
Anti-IFN-γ-treated mice — a model for testing safety of live Salmonella vaccines
Muotiala, A. (1992) · Vaccine · doi:10.1016/0264-410x(92)90159-h · Cited by 18

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Authors: Burton, N. A., Schürmann, N., Casse, O., Steeb, A. K., Claudi, B., Zankl, J., Schmidt, A., & Bumann, D.
Affiliations: University of Basel (CH)
Corresponding author: Bumann, Dirk
ORCID: Claudi, Beatrice
Schmidt, Alexander
Bumann, Dirk
Venue: Cell Host & Microbe
Publisher: Elsevier BV
Published: 2014-01
Volume: 15
Issue: 1
Pages: 72-83
ISSN: 1931-3128 (ISSN-L)
DOI: 10.1016/j.chom.2013.12.006
OpenAlex: W2034408518
Cited by: 175
References: 77
Citations by year: 2026: 8 · 2025: 13 · 2024: 13 · 2023: 9 · 2022: 11 · 2021: 15 · 2020: 17 · 2019: 17 · 2018: 9 · 2017: 19 · 2016: 15 · 2015: 19 · 2014: 10
FWCI: 9.59
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 462 d)
Locations: Cell Host & Microbe (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft (SPP 1316)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Agricultural and Biological Sciences › Food Science › Salmonella and Campylobacter epidemiology
Keywords: Salmonella, reactive oxygen species, reactive nitrogen species, oxidative stress, nitrosative stress, host-pathogen interaction, neutrophils, inflammatory monocytes, NADPH oxidase, myeloperoxidase, red pulp macrophages, inducible nitric oxide synthase, single-cell tracking, systemic infection, spleen, mouse model
MeSH terms: Animals, Female, Macrophages, Monocytes, Peroxidase, Neutrophils, Oxygenases, Salmonella Infections, Salmonella typhimurium, Spleen, Gene Expression, Respiratory Burst, Reactive Oxygen Species, NADPH Oxidases, Reactive Nitrogen Species, Mice, Nitric Oxide Synthase Type II, Host-Pathogen Interactions, Single-Cell Analysis

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Disparate Impact of Oxidative Host Defenses Determines the Fate of Salmonella during Systemic Infection in Mice

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