Cited by 329Neutrophil, Myeloperoxidase and Oxidative MechanismsImmunotherapy and Immune ResponsesRedox biology and oxidative stress

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

NADPH oxidase controls phagosomal pH and antigen cross-presentation in human dendritic cells

Open access

Mantegazza, Adriana R., Savina, Ariel, Vermeulen, Mónica, Pérez, Laura, Geffner, Jorge, Hermine, Olivier, Rosenzweig, Sergio D., Faure, Florence, Amigorena, Sebastián·2008·Blood

DOI 10.1182/blood-2008-01-134791PMC PMC2597138

Open this paper in CoChat — free account Open PDF

Abstract

The phagocyte NADPH oxidase (NOX2) is critical for the bactericidal activity of phagocytic cells and plays a major role in innate immunity. We showed recently that NOX2 activity in mouse dendritic cells (DCs) prevents acidification of phagosomes, promoting antigen cross-presentation. Inorder to investigate the role of NOX2 in the regulation of the phagosomal pH in human DCs, we analyzed the production of reactive oxygen species (ROS) and the phagosomal/endosomal pH in monocyte-derived DCs and macrophages (MØs) from healthy donors or patients with chronic granulomatous disease (CGD). As expected, we found that human MØs acidify their phagosomes more efficiently than human DCs. Accordingly, the expression of the vacuolar proton ATPase (V-H+-ATPase) was higher in MØs than in DCs. Phagosomal ROS production, however, was also higher in MØs than in DCs, due to higher levels of gp91phox expression and recruitment to phagosomes. In contrast, in the absence of active NOX2, the phagosomal and endosomal pH decreased. Both in the presence of a NOX2 inhibitor and in DCs derived from patients with CGD, the cross-presentation of 2 model tumor antigens was impaired. We conclude that NOX2 activity participates in the regulation of the phagosomal and endosomal pH in human DCs, and is required for efficient antigen cross-presentation.

Integrity signals

Registry

Crossref · 10.1182/blood-2008-01-134791

Cites

34 of 34 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Modulating Innate and Adaptive Immunity by (R)-Roscovitine: Potential Therapeutic Opportunity in Cystic Fibrosis
Meijer, L., Nelson, D. J., Riazanski, V., Gabdoulkhakova, A. G., Héry-Arnaud, G., Berre, R. L., Loaëc, N., Oumata, N., Galons, H., Nowak, E., et al. (2016) · Journal of Innate Immunity · doi:10.1159/000444256 · Cited by 5,008
Toll-like receptor 4–dependent contribution of the immune system to anticancer chemotherapy and radiotherapy
Apetoh, L., Ghiringhelli, F., Tesniere, A., Obeid, M., Ortiz, C., Criollo, A., Mignot, G., Maiuri, M. C., Ullrich, E., Saulnier, P., et al. (2007) · Nature Medicine · doi:10.1038/nm1622 · Cited by 3,056
Self-citation
NOX2 Controls Phagosomal pH to Regulate Antigen Processing during Crosspresentation by Dendritic Cells
Savina, A., Jancic, C. C., Hugues, S., Guermonprez, P., Vargas, P., Moura, I. C., Lennon‐Duménil, A., Seabra, M. C., Raposo, G., & Amigorena, S. (2006) · Cell · doi:10.1016/j.cell.2006.05.035 · Cited by 896
Self-citation
Cross-Presentation, Dendritic Cells, Tolerance and Immunity
Heath, W. R., & Carbone, F. R. (2001) · Annual Review of Immunology · doi:10.1146/annurev.immunol.19.1.47 · Cited by 882
Differential Lysosomal Proteolysis in Antigen-Presenting Cells Determines Antigen Fate
Delamarre, L., Pack, M., Chang, H. C., Mellman, I., & Trombetta, E. S. (2005) · Science · doi:10.1126/science.1108003 · Cited by 776
ER–phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
Guermonprez, P., Saveanu, L., Kleijmeer, M. J., Davoust, J. M., Endert, P. V., & Amigorena, S. (2003) · Nature · doi:10.1038/nature01911 · Cited by 753
Self-citation
Selective transport of internalized antigens to the cytosol for MHC class I presentation in dendritic cells
Rodrı́guez, A., Régnault, A., Kleijmeer, M. J., Ricciardi‐Castagnoli, P., & Amigorena, S. (1999) · Nature Cell Biology · doi:10.1038/14058 · Cited by 552
Self-citation
CFTR regulates phagosome acidification in macrophages and alters bactericidal activity
Di, A., Brown, M. E., Deriy, L. V., Li, C., Szeto, F. L., Chen, Y., Huang, P. C., Tong, J., Naren, A. P., Bindokas, V. P., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1456 · Cited by 516
The NADPH oxidase of professional phagocytes—prototype of the NOX electron transport chain systems
Cross, A. R., & Segal, A. W. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.03.008 · Cited by 489
Cross‐presentation: underlying mechanisms and role in immune surveillance
Rock, K. L., & Shen, L. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00301.x · Cited by 469

Show all 34 references

Sorted by citations

Cross-presentation by dendritic cells
Joffre, O. P., Segura, É., Savina, A., & Amigorena, S. (2012) · Nature reviews. Immunology · doi:10.1038/nri3254 · Cited by 1,764
Self-citation
Reactive oxygen species and mitochondria: A nexus of cellular homeostasis
Dunn, J. D., Álvarez, L., Zhang, X., & Soldati, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.005 · Cited by 1,233
The Cell Biology of Phagocytosis
Flannagan, R. S., Jaumouillé, V., & Grinstein, S. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011811-132445 · Cited by 1,100
Redox regulation of the immune response
Morris, G., Gevezova, M., Sarafian, V. S., & Maes, M. H. J. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00902-0 · Cited by 628
Are Reactive Oxygen Species Always Detrimental to Pathogens?
Paiva, C. N., & Bozza, M. T. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5447 · Cited by 577
Activation of antibacterial autophagy by NADPH oxidases
Huang, J., Canadien, V., Lam, G. Y., Steinberg, B. E., Dinauer, M. C., Magalhaes, M. A. O., Glogauer, M., Grinstein, S., & Brumell, J. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811045106 · Cited by 556
Reactive Oxygen Species in the Immune System
Yang, Y., Bazhin, A. V., Werner, J., & Karakhanova, S. (2013) · International Reviews of Immunology · doi:10.3109/08830185.2012.755176 · Cited by 523
Current Concepts of Antigen Cross-Presentation
Embgenbroich, M., & Burgdorf, S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01643 · Cited by 429
The Role of Macrophages in Staphylococcus aureus Infection
Pidwill, G. R., Gibson, J. F., Cole, J., Renshaw, S. A., & Foster, S. J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.620339 · Cited by 360
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342
Reactive Oxygen Species Regulate T Cell Immune Response in the Tumor Microenvironment
Chen, X., Song, M., Zhang, B., & Zhang, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1580967 · Cited by 326
The life cycle of phagosomes: formation, maturation, and resolution
Levin‐Konigsberg, R., Grinstein, S., & Canton, J. (2016) · Immunological Reviews · doi:10.1111/imr.12439 · Cited by 328
Dendritic Cells but Not Macrophages Sense Tumor Mitochondrial DNA for Cross-priming through Signal Regulatory Protein α Signaling
Xu, M. M., Yang, P., Han, D., Shi, Y., Cao, X., Liang, H. L., Chen, X., Li, X.-D., Deng, L., Chen, Z. J., et al. (2017) · Immunity · doi:10.1016/j.immuni.2017.07.016 · Cited by 315
The Small GTPase Rac2 Controls Phagosomal Alkalinization and Antigen Crosspresentation Selectively in CD8+ Dendritic Cells
Savina, A., Peres, A., Cebrián, I., Carmo, N., Moita, C. F., Hacohen, N., Moita, L. F., & Amigorena, S. (2009) · Immunity · doi:10.1016/j.immuni.2009.01.013 · Cited by 306
Self-citation
The Biology and Underlying Mechanisms of Cross-Presentation of Exogenous Antigens on MHC-I Molecules
Cruz, F. M., Colbert, J. D., Merino, E., Kriegsman, B. A., & Rock, K. L. (2017) · Annual Review of Immunology · doi:10.1146/annurev-immunol-041015-055254 · Cited by 321
Oxidative Stress in the Tumor Microenvironment and Its Relevance to Cancer Immunotherapy
Aboelella, N. S., Brandle, C., Kim, T., Ding, Z., & Zhou, G. (2021) · Cancers · doi:10.3390/cancers13050986 · Cited by 303
Similar antigen cross-presentation capacity and phagocytic functions in all freshly isolated human lymphoid organ–resident dendritic cells
Segura, É., Durand, M., & Amigorena, S. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20121103 · Cited by 313
Self-citation
Nanoparticle Drug Delivery Systems Designed to Improve Cancer Vaccines and Immunotherapy
Fan, Y., & Moon, J. J. (2015) · Vaccines · doi:10.3390/vaccines3030662 · Cited by 278
Acid Resistance inMycobacterium tuberculosis
Vandal, O. H., Nathan, C., & Ehrt, S. (2009) · Journal of Bacteriology · doi:10.1128/jb.00305-09 · Cited by 261
Presentation of Phagocytosed Antigens by MHC Class I and II
Mantegazza, A. R., Magalhaes, J. G., Amigorena, S., & Marks, M. S. (2012) · Traffic · doi:10.1111/tra.12026 · Cited by 289
Self-citation
Antigen Cross-Presentation by Macrophages
Muntjewerff, E. M., Meesters, L. D., & van den Bogaart, G. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01276 · Cited by 262
Induction of regulatory T cells by macrophages is dependent on production of reactive oxygen species
Kraaij, M. D., Savage, N. D. L., van der Kooij, S. W., Koekkoek, K. M., Wang, J., van den Berg, J. M., Ottenhoff, T. H. M., Kuijpers, T. W., Holmdahl, R., van Kooten, C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012016107 · Cited by 259
Intracellular mechanisms of antigen cross presentation in dendritic cells
Amigorena, S., & Savina, A. (2010) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.01.022 · Cited by 264
Self-citation
The many roles of NOX2 NADPH oxidase-derived ROS in immunity
Lam, G. Y., Huang, J., & Brumell, J. H. (2010) · Seminars in Immunopathology · doi:10.1007/s00281-010-0221-0 · Cited by 251
The effects of neutrophil-generated hypochlorous acid and other hypohalous acids on host and pathogens
Ulfig, A., & Leichert, L. I. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03591-y · Cited by 239
The protective role of ROS in autoimmune disease
Hultqvist, M. H., Olsson, L. M., Gelderman, K. A., & Holmdahl, R. (2009) · Trends in Immunology · doi:10.1016/j.it.2009.03.004 · Cited by 228
Contrasting phagosome pH regulation and Maturation in Human M1 and M2 macrophages
Canton, J., Khezri, R., Glogauer, M., & Grinstein, S. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-05-0967 · Cited by 221
The Influence of Gut Microbiota on Oxidative Stress and the Immune System
Kunst, C., Schmid, S. A., Michalski, M., Tümen, D., Buttenschoen, J., Müller, M., & Gülow, K. (2023) · Biomedicines · doi:10.3390/biomedicines11051388 · Cited by 240
NOX2-dependent regulation of inflammation
Singel, K. L., & Segal, B. H. (2016) · Clinical Science · doi:10.1042/cs20150660 · Cited by 224
Activation of caspase-1 by the NLRP3 inflammasome regulates the NADPH oxidase NOX2 to control phagosome function
Sokolovska, A., Becker, C., Ip, W., Rathinam, V. A. K., Brudner, M., Paquette, N., Tanne, A. J., Vanaja, S. K., Moore, K. J., Fitzgerald, K. A., et al. (2013) · Nature Immunology · doi:10.1038/ni.2595 · Cited by 205
Regulation of the NADPH Oxidase and Associated Ion Fluxes During Phagocytosis
Nunes, P., Demaurex, N., & Dinauer, M. C. (2013) · Traffic · doi:10.1111/tra.12115 · Cited by 204
Eat Prey, Live: Dictyostelium discoideum As a Model for Cell-Autonomous Defenses
Dunn, J. D., Bosmani, C., Barisch, C., Raykov, L., Lefrançois, L. H., Cardenal‐Muñoz, E., López-Jiménez, A. T., & Soldati, T. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01906 · Cited by 199
Antigen delivery to early endosomes eliminates the superiority of human blood BDCA3+ dendritic cells at cross presentation
Cohn, L. B., Chatterjee, B., Esselborn, F., Smed‐Sörensen, A., Nakamura, N., Chalouni, C. M., Lee, B.-C., Vandlen, R. A., Keler, T., Lauer, P., et al. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20121251 · Cited by 200
Antigen processing and presentation
(2019) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2019.07.005 · Cited by 194
Regulation of the Cell Biology of Antigen Cross-Presentation
Blander, J. M. (2018) · Annual Review of Immunology · doi:10.1146/annurev-immunol-041015-055523 · Cited by 206
V-ATPase is a universal regulator of LC3-associated phagocytosis and non-canonical autophagy
Hooper, K. M., Jacquin, É., Li, T., Goodwin, J. M., Brumell, J. H., Durgan, J., & Florey, O. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202105112 · Cited by 193
Toll-like Receptor 4 Engagement on Dendritic Cells Restrains Phago-Lysosome Fusion and Promotes Cross-Presentation of Antigens
Alloatti, A., Kotsias, F., Pauwels, A.-M., Carpier, J.-M., Jouve, M. J., Timmerman, E., Pace, L., Vargas, P., Maurin, M., Gehrmann, U., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.11.006 · Cited by 189
Self-citation
Lupus-associated causal mutation in neutrophil cytosolic factor 2 (NCF2) brings unique insights to the structure and function of NADPH oxidase
Jacob, C. O., Eisenstein, M., Dinauer, M. C., Ming, W., Liu, Q., John, S. K., Quismorio, F. P., Reiff, A. O., Myones, B. L., Kaufman, K. M., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113251108 · Cited by 183
Targeting dendritic cells: a promising strategy to improve vaccine effectiveness
Macri, C., Dumont, C., Johnston, A. P. R., & Mintern, J. D. (2016) · Clinical & Translational Immunology · doi:10.1038/cti.2016.6 · Cited by 187
Many roads lead to CASM: Diverse stimuli of noncanonical autophagy share a unifying molecular mechanism
Durgan, J., & Florey, O. (2022) · Science Advances · doi:10.1126/sciadv.abo1274 · Cited by 181
Cross-presentation of cell-associated antigens by MHC class I in dendritic cell subsets
Gutiérrez-Martínez, E. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00363 · Cited by 191
The role of NADPH oxidases in infectious and inflammatory diseases
Taylor, J. P., & Tse, H. M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102159 · Cited by 185
Prolonged Production of Reactive Oxygen Species in Response to B Cell Receptor Stimulation Promotes B Cell Activation and Proliferation
Wheeler, M. L., & DeFranco, A. L. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201433 · Cited by 175
Roles of reactive oxygen species in inflammation and cancer
Yu, Y., Liu, S., Yang, L., Song, P., Liu, Z., Liu, X., Yan, X., & Dong, Q. (2024) · MedComm · doi:10.1002/mco2.519 · Cited by 180
Leishmania promastigotes: building a safe niche within macrophages
Moradin, N., & Descoteaux, A. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00121 · Cited by 157
Lipid peroxidation causes endosomal antigen release for cross-presentation
Dingjan, I., Verboogen, D. R. J., Paardekooper, L. M., Revelo, N. H., Sittig, S. P., Visser, L. J., von Mollard, G. F., Henriet, S., Figdor, C. G., ter Beest, M., et al. (2016) · Scientific Reports · doi:10.1038/srep22064 · Cited by 153
Reactive Oxygen Species and Antitumor Immunity—From Surveillance to Evasion
Kotsafti, A., Scarpa, M., Castagliuolo, I., & Scarpa, M. (2020) · Cancers · doi:10.3390/cancers12071748 · Cited by 161
NADPH oxidase activity controls phagosomal proteolysis in macrophages through modulation of the lumenal redox environment of phagosomes
Rybicka, J. M., Balce, D. R., Khan, M. F., Krohn, R. M., & Yates, R. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914867107 · Cited by 153
Dendritic Cell-Based Vaccines: Barriers and Opportunities
Cintolo, J. A., Datta, J., Mathew, S., & Czerniecki, B. J. (2012) · Future Oncology · doi:10.2217/fon.12.125 · Cited by 157
IFN-α enhances cross-presentation in human dendritic cells by modulating antigen survival, endocytic routing, and processing
Spadaro, F., Lapenta, C., Donati, S., Abalsamo, L., Barnaba, V., Belardelli, F., Santini, S. M., & Ferrantini, M. (2011) · Blood · doi:10.1182/blood-2011-06-363564 · Cited by 150
Phagosomal proteolysis in dendritic cells is modulated by NADPH oxidase in a pH‐independent manner
Rybicka, J. M., Balce, D. R., Chaudhuri, S., Allan, E. R. O., & Yates, R. M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.440 · Cited by 141
Endoplasmic Reticulum Stress and Nox-Mediated Reactive Oxygen Species Signaling in the Peripheral Vasculature: Potential Role in Hypertension
Santos, C. X. C., Nabeebaccus, A., Shah, A. M., Camargo, L. L., Filho, S. V., & Lopes, L. R. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5262 · Cited by 143
Reactive Oxygen Species Production in the Phagosome: Impact on Antigen Presentation in Dendritic Cells
Kotsias, F., Hoffmann, E., Amigorena, S., & Savina, A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4557 · Cited by 142
Self-citation
Precise modulation and use of reactive oxygen species for immunotherapy
Li, X., Gao, J., Wu, C., Wang, C., Zhang, R., He, J., Xia, Z. J., Joshi, N., Karp, J. M., & Kuai, R. (2024) · Science Advances · doi:10.1126/sciadv.adl0479 · Cited by 140
Regulation of innate immunity by NADPH oxidase
Segal, B. H., Grimm, M. J., Khan, A. N. H., Han, W., & Blackwell, T. S. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.022 · Cited by 140
Mammalian NADPH Oxidases
Buvelot, H., Jaquet, V., & Krause, K. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9424-3_2 · Cited by 136
From Flies to Men: ROS and the NADPH Oxidase in Phagocytes
Moghadam, Z. M., Henneke, P., & Kolter, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.628991 · Cited by 146
Ncf1 polymorphism reveals oxidative regulation of autoimmune chronic inflammation
Holmdahl, R., Sareila, O., Olsson, L. M., Bäckdahl, L., & Wing, K. (2016) · Immunological Reviews · doi:10.1111/imr.12378 · Cited by 131
Beyond cDC1: Emerging Roles of DC Crosstalk in Cancer Immunity
Noubade, R., Majri-Morrison, S. S., & Tarbell, K. V. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01014 · Cited by 134
Determinants, maintenance, and function of organellar pH
Freeman, S. A., Grinstein, S., & Orlowski, J. (2022) · Physiological Reviews · doi:10.1152/physrev.00009.2022 · Cited by 127
Better Together: Current Insights Into Phagosome-Lysosome Fusion
Nguyen, J. A., & Yates, R. M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.636078 · Cited by 135
The Role of FcRn in Antigen Presentation
Baker, K., Räth, T., Pyzik, M., & Blumberg, R. S. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00408 · Cited by 123
Cross-Presentation in Mouse and Human Dendritic Cells
Segura, É., & Amigorena, S. (2015) · Advances in immunology · doi:10.1016/bs.ai.2015.03.002 · Cited by 131
Self-citation
DAMPs and inflammatory processes: the role of redox in the different outcomes
Carta, S., Castellani, P., Delfino, L., Tassi, S., Venè, R., & Rubartelli, A. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.1008598 · Cited by 112
Reactive Oxygen Species Produced by the NADPH Oxidase 2 Complex in Monocytes Protect Mice from Bacterial Infections
Pizzolla, A., Hultqvist, M., Nilson, B., Grimm, M. J., Eneljung, T., Jonsson, I.-M., Verdrengh, M., Kelkka, T., Gjertsson, I., Segal, B. H., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103430 · Cited by 108
Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with Dextran
Pustylnikov, S., Sagar, D., Jain, P., & Khan, Z. K. (2014) · Journal of Pharmacy & Pharmaceutical Sciences · doi:10.18433/j3n590 · Cited by 105
Hydroxychloroquine inhibits proinflammatory signalling pathways by targeting endosomal NADPH oxidase
Müller‐Calleja, N., Manukyan, D., Canisius, A., Strand, D. J., & Lackner, K. J. (2016) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2016-210012 · Cited by 110
Lysosome remodelling and adaptation during phagocyte activation
Hipolito, V. E. B., Escobar, E. O., & Botelho, R. J. (2018) · Cellular Microbiology · doi:10.1111/cmi.12824 · Cited by 103
Mycobacteria and the Intraphagosomal Environment: Take It With a Pinch of Salt(s)!
Soldati, T., & Neyrolles, O. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01358.x · Cited by 111
Metabolic adaptation supports enhanced macrophage efferocytosis in limited-oxygen environments
Wang, Y., Trzeciak, A. J., Rojas, W. S., Saavedra, P. H. V., Chen, Y., Chirayil, R., Etchegaray, J. I., Lucas, C. D., Puleston, D. J., Keshari, K. R., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.12.005 · Cited by 110
Phagosome maturation in polarized macrophages
Canton, J. (2014) · Journal of Leukocyte Biology · doi:10.1189/jlb.1mr0114-021r · Cited by 115
NADPH oxidase modifies patterns of MHC class II–restricted epitopic repertoires through redox control of antigen processing
Allan, E. R. O., Tailor, P., Balce, D. R., Pirzadeh, P., McKenna, N. T., Renaux, B., Warren, A. L., Jirik, F. R., & Yates, R. M. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302896 · Cited by 95
MHC molecules and microbial antigen processing in phagosomes
Ramachandra, L., Simmons, D. P., & Harding, C. V. (2009) · Current Opinion in Immunology · doi:10.1016/j.coi.2009.01.001 · Cited by 95
The Plasma Membrane: A Platform for Intra- and Intercellular Redox Signaling
Nordzieke, D. E., & Medraño-Fernandez, I. (2018) · Antioxidants · doi:10.3390/antiox7110168 · Cited by 90
Staphylococcus aureus, phagocyte NADPH oxidase and chronic granulomatous disease
Buvelot, H., Posfay-Barbe, K. M., Linder, P., Schrenzel, J., & Krause, K. (2016) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuw042 · Cited by 92
Autologous Dendritic Cells Prolong Allograft Survival Through Tmem176b-Dependent Antigen Cross-Presentation
Segovia, M., Louvet, C., Charnet, P., Savina, A., Tilly, G., Gautreau‐Rolland, L., Carretero-Iglesia, L., Bériou, G., Cebrián, I., Cens, T., et al. (2014) · American Journal of Transplantation · doi:10.1111/ajt.12708 · Cited by 89
Self-citation
Oxygen in the tumor microenvironment: effects on dendritic cell function
Paardekooper, L. M., de Vos, W., & van den Bogaart, G. (2019) · Oncotarget · doi:10.18632/oncotarget.26608 · Cited by 89
Phagocyte NADPH oxidase and specific immunity
Cachat, J., Deffert, C., Hugues, S., & Krause, K. (2015) · Clinical Science · doi:10.1042/cs20140635 · Cited by 89
Deletion of nuoG from the Vaccine Candidate Mycobacterium bovis BCG Δ ureC :: hly Improves Protection against Tuberculosis
Gengenbacher, M., Nieuwenhuizen, N. E., Vogelzang, A., Liu, H., Kaiser, P., Schuerer, S., Lazar, D., Wagner, I., Mollenkopf, H., & Kaufmann, S. H. E. (2016) · mBio · doi:10.1128/mbio.00679-16 · Cited by 87
Adaptor Protein-3 in Dendritic Cells Facilitates Phagosomal Toll-like Receptor Signaling and Antigen Presentation to CD4+ T Cells
Mantegazza, A. R., Guttentag, S. H., Benna, J. E., Sasai, M., Iwasaki, A., Shen, H., Laufer, T. M., & Marks, M. S. (2012) · Immunity · doi:10.1016/j.immuni.2012.02.018 · Cited by 79
Self-citation
NADPH oxidase activation regulates apoptotic neutrophil clearance by murine macrophages
Bagaitkar, J., Huang, J., Zeng, M. Y., Pech, N. K., Monlish, D. A., Perez‐Zapata, L. J., Miralda, I., Schuettpelz, L. G., & Dinauer, M. C. (2018) · Blood · doi:10.1182/blood-2017-09-809004 · Cited by 83
Mechanisms by Which Dendritic Cells Present Tumor Microparticle Antigens to CD8+ T Cells
Ma, J., Wei, K., Zhang, H., Tang, K., Li, F., Zhang, T., Liu, J., Xu, P., Yu, Y., Sun, W., et al. (2018) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-17-0716 · Cited by 79
Quantum Sensing of Free Radicals in Primary Human Dendritic Cells
Nie, L., Nusantara, A. C., Damle, V. G., Baranov, M. V., Chipaux, M., Reyes-San-Martin, C., Hamoh, T., Epperla, C. P., Guricova, M., Cígler, P., et al. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c03021 · Cited by 78
CD4+ T cell vaccination overcomes defective cross-presentation of fungal antigens in a mouse model of chronic granulomatous disease
Luca, A. D., Iannitti, R. G., Bozza, S., Beau, R., Casagrande, A., D’Angelo, C., Moretti, S., Cunha, C., Giovannini, G., Massi-Benedetti, C., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci60862 · Cited by 77
Reactive oxygen species in immune cells: A new antitumor target
Wang, L., Kuang, Z., Zhang, D., Gao, Y., Ying, M., & Wang, T. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110978 · Cited by 81
Defining the Roles of Human Carcinoembryonic Antigen-Related Cellular Adhesion Molecules during Neutrophil Responses to Neisseria gonorrhoeae
Sarantis, H., & Gray‐Owen, S. D. (2011) · Infection and Immunity · doi:10.1128/iai.05702-11 · Cited by 74
miR-24, miR-30b and miR-142-3p interfere with antigen processing and presentation by primary macrophages and dendritic cells
Naqvi, A. R., Fordham, J. B., Ganesh, B. B., & Nares, S. (2016) · Scientific Reports · doi:10.1038/srep32925 · Cited by 76
Antitumor immune responses mediated by dendritic cells: How signals derived from dying cancer cells drive antigen cross-presentation
Spel, L., Boelens, J. J., Nierkens, S., & Boes, M. L. (2013) · OncoImmunology · doi:10.4161/onci.26403 · Cited by 77
A Modular and Combinatorial View of the Antigen Cross‐Presentation Pathway in Dendritic Cells
Segura, É., & Villadangos, J. A. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01254.x · Cited by 73
Human Intestinal Mononuclear Phagocytes in Health and Inflammatory Bowel Disease
Caër, C., & Wick, M. J. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00410 · Cited by 76
Antigen Presentation in the Lung
Kawasaki, T., Ikegawa, M., & Kawai, T. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.860915 · Cited by 78
Inflammatory consequences of inherited disorders affecting neutrophil function
Dinauer, M. C. (2019) · Blood · doi:10.1182/blood-2018-11-844563 · Cited by 72
Neutrophils acquire antigen-presenting cell features after phagocytosis of IgG-opsonized erythrocytes
Meinderts, S. M., Baker, G., van Wijk, S. W., Beuger, B. M., Geissler, J., Jansen, M. H., Saris, A., ten Brinke, A., Kuijpers, T. W., van den Berg, T. K., et al. (2019) · Blood Advances · doi:10.1182/bloodadvances.2018028753 · Cited by 68
From immunology to artificial intelligence: revolutionizing latent tuberculosis infection diagnosis with machine learning
Li, L., Yang, L., Li, Z., Ye, Z., Zhao, W., & Gong, W. (2023) · Military Medical Research · doi:10.1186/s40779-023-00490-8 · Cited by 80
Human Monocyte-Derived Dendritic Cells Produce Millimolar Concentrations of ROS in Phagosomes Per Second
Paardekooper, L. M., Dingjan, I., Linders, P. T. A., Staal, A. H. J., Cristescu, S. M., Verberk, W. C. E. P., & van den Bogaart, G. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01216 · Cited by 69
Uptake of Particulate Antigens in a Nonmammalian Lung: Phenotypic and Functional Characterization of Avian Respiratory Phagocytes Using Bacterial or Viral Antigens
de Geus, E. D., Jansen, C. A., & Vervelde, L. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200092 · Cited by 68
Perforin-2 is a pore-forming effector of endocytic escape in cross-presenting dendritic cells
Rodríguez-Silvestre, P., Laub, M., Krawczyk, P. A., Davies, A. K., Schessner, J. P., Parveen, R., Tuck, B. J., McEwan, W. A., Borner, G. H. H., & Kozik, P. (2023) · Science · doi:10.1126/science.adg8802 · Cited by 75
Redox signaling in innate immunity and inflammation: focus on macrophages and neutrophils
Braunstein, I., Motohashi, H., Dallenga, T. K., Schaible, U. E., & Benhar, M. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.06.006 · Cited by 75
Pathways of MHC I cross-presentation of exogenous antigens
Cruz, F. M., Chan, A., & Rock, K. L. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101729 · Cited by 66
Protein Disulfide Isomerase and Host-Pathogen Interaction
Stolf, B. S., Smyrnias, I., Lopes, L. R., Gatti, A. V., Goto, H., Laurindo, F. R. M., Shah, A. M., & Santos, C. X. C. (2011) · The Scientific World JOURNAL · doi:10.1100/2011/289182 · Cited by 66

Authors: Mantegazza, A. R., Savina, A., Vermeulen, M., Pérez, L., Geffner, J., Hermine, O., Rosenzweig, S. D., Faure, F., & Amigorena, S.
Affiliations: Inserm (FR)
Instituto de Investigaciones Hematológicas, Academia Nacional de Medicina, Buenos Aires, Argentina;
Garrahan Hospital (AR)
Academia Nacional de Medicina (AR)
Hôpital Necker-Enfants Malades (FR)
ORCID: Mantegazza, Adriana R.
Pérez, Laura
Geffner, Jorge
Hermine, Olivier
Rosenzweig, Sergio D.
Faure, Florence
Amigorena, Sebastián
Venue: Blood
Publisher: American Society of Hematology
Published: 2008-12-01
Volume: 112
Issue: 12
Pages: 4712-4722
ISSN: 0006-4971 (ISSN-L)
1528-0020
DOI: 10.1182/blood-2008-01-134791
PMC: PMC2597138
OpenAlex: W2093168274
Cited by: 329
References: 34
Citations by year: 2026: 14 · 2025: 16 · 2024: 17 · 2023: 26 · 2022: 23 · 2021: 22 · 2020: 28 · 2019: 17 · 2018: 22 · 2017: 18 · 2016: 15 · 2015: 18 · 2014: 8 · 2013: 15 · 2012: 28
FWCI: 5.84
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Blood (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
CONICET Digital (CONICET) (submittedVersion, cc-by-nc-sa)
Funders: Institut National de la Santé et de la Recherche Médicale
Consejo Nacional de Investigaciones Científicas y Técnicas
National Institutes of Health
Directorate for Biological Sciences
Fogarty International Center (R01TW006644)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: NADPH oxidase, NOX2, dendritic cells, phagosomal pH, cross-presentation, reactive oxygen species, gp91phox, vacuolar ATPase, chronic granulomatous disease, monocyte-derived macrophages, endosomal pH, innate immunity
MeSH terms: NADPH Oxidase 2, Acid-Base Equilibrium, Adolescent, Adult, Cells, Cultured, Child, Child, Preschool, Dendritic Cells, Humans, Hydrogen-Ion Concentration, Macrophages, Membrane Glycoproteins, Phagosomes, Antigen Presentation, NADPH Oxidases, Cross-Priming, Young Adult

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

NADPH oxidase controls phagosomal pH and antigen cross-presentation in human dendritic cells

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks