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Transcriptional Adaptation of Mycobacterium tuberculosis within Macrophages
Open accessAbstract
Little is known about the biochemical environment in phagosomes harboring an infectious agent. To assess the state of this organelle we captured the transcriptional responses of Mycobacterium tuberculosis (MTB) in macrophages from wild-type and nitric oxide (NO) synthase 2–deficient mice before and after immunologic activation. The intraphagosomal transcriptome was compared with the transcriptome of MTB in standard broth culture and during growth in diverse conditions designed to simulate features of the phagosomal environment. Genes expressed differentially as a consequence of intraphagosomal residence included an interferon γ– and NO-induced response that intensifies an iron-scavenging program, converts the microbe from aerobic to anaerobic respiration, and induces a dormancy regulon. Induction of genes involved in the activation and β-oxidation of fatty acids indicated that fatty acids furnish carbon and energy. Induction of σE-dependent, sodium dodecyl sulfate–regulated genes and genes involved in mycolic acid modification pointed to damage and repair of the cell envelope. Sentinel genes within the intraphagosomal transcriptome were induced similarly by MTB in the lungs of mice. The microbial transcriptome thus served as a bioprobe of the MTB phagosomal environment, showing it to be nitrosative, oxidative, functionally hypoxic, carbohydrate poor, and capable of perturbing the pathogen's cell envelope.
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“Several studies have reported that nuo is down-regulated in M. tuberculosis during mouse lung infection (18), survival in macrophages (19), in both non-replicating persistence (NRP)-1 (1% oxygen saturation) and NRP-2 (0.06% oxygen saturation) relative to aerated mid-log growth (18), and upon starvation in vitro (20).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [19]
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“In contrast, fumarate reductase, nitrate reductase and NDH-2 are all upregulated under these conditions (19).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [19]
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“Transcriptional analysis of M. tuberculosis in the macrophage (phagosomal environment) has revealed that NDH-1, menaquinol-cytochrome c oxidoreductase and the ATP synthase are all down-regulated when compared to cells growing exponentially, suggesting that there is a reduced need for energy generation during bacteriostasis i.e., the growth state of intraphagosomal M. tuberculosis (19).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [19]
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“In M. tuberculosis, the atp operon is downregulated during growth in macrophages (19), the mouse lung and in cells exposed to NO or hypoxia (18).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [19]
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“the fight of the host against the pathogen in M. tuberculosis infection involves several levels including containment of the microbe, generation of radicals and a hostile, acidic environment, deprivation from essential nutrients, formation of anti-mycobacterial peptides and cytokines which strengthen host responses by attracting other immune cells, down to cell damage and suicidal activities of MO”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [5]
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“Accordingly, transcriptional analysis of macrophages and M. tuberculosis has demonstrated that Mycobacteria regulate a myriad of genes to secure a sufficient supply of iron within the cell, whereas macrophages aim to restrict the availability of this metal by different mechanisms (5).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [5]
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Cites
In silico prediction of protein-protein interactions in human macrophages
Souiai, O., Guerfali, F. Z., Miled, S. B., Brun, C., & Benkahla, A. (2014) · BMC Research Notes · doi:10.1186/1756-0500-7-157 · Cited by 10,785
Significance analysis of microarrays applied to the ionizing radiation response
Tusher, V. G., Tibshirani, R., & Chu, G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091062498 · Cited by 10,568
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
Mechanisms of phagocytosis in macrophages
Aderem, A., & Underhill, D. M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.593 · Cited by 2,854
Escherichia coli and Salmonella.
Neidhart, F. C. (1996) · Cited by 1,577
Common themes in microbial pathogenicity revisited
Finlay, B. B., & Falkow, S. (1997) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.61.2.136-169.1997 · Cited by 1,474
Nathan, C., & Shiloh, M. U. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.8841 · Cited by 1,469
Self-citationBetts, J. C., Lukey, P. T., Robb, L. C., McAdam, R. A., & Duncan, K. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02779.x · Cited by 1,395
McKinney, J. D., zu Bentrup, K. H., Muñoz‐Elías, E. J., Miczák, A., Chen, B., Chan, W.-T., Swenson, D. L., Sacchettini, J. C., Jacobs, W. R., & Russell, D. G. (2000) · Nature · doi:10.1038/35021074 · Cited by 1,361
Flynn, J., & Chan, J. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.19.1.93 · Cited by 1,144
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Humphrys, M. S., Creasy, T. H., Sun, Y., Shetty, A. C., Chibucos, M. C., Drábek, E. F., Fraser, C. M., Farooq, U., Sengamalay, N. A., Ott, S., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080597 · Cited by 128
Reddy, P. V., Puri, R. V., Chauhan, P., Kar, R., Rohilla, A., Khera, A., & Tyagi, A. K. (2013) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit250 · Cited by 127
Taneja, N. K., Dhingra, S., Mittal, A., Naresh, M., & Tyagi, J. S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010860 · Cited by 129
Energetics of Pathogenic Bacteria and Opportunities for Drug Development
Cook, G. M., Greening, C., Hards, K., & Berney, M. (2014) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2014.08.001 · Cited by 129
A High-Throughput Screen for Tuberculosis Progression
Carvalho, R., de Sonneville, J., Stockhammer, O. W., Savage, N. D. L., Veneman, W. J., Ottenhoff, T. H. M., Dirks, R. P., Meijer, A. H., & Spaink, H. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016779 · Cited by 126
Chewing the fat: lipid metabolism and homeostasis during M. tuberculosis infection
Lovewell, R. R., Sassetti, C. M., & VanderVen, B. C. (2015) · Current Opinion in Microbiology · doi:10.1016/j.mib.2015.10.002 · Cited by 131
Krieger, I. V., Freundlich, J. S., Gawandi, V., Roberts, J. P., Gawandi, V. B., Sun, Q., Owen, J. L., Fraile, M., Huss, S. I., Lavandera, J.-L., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.09.018 · Cited by 125
Raman, S., Hazra, R., Dascher, C. C., & Husson, R. N. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.19.6605-6616.2004 · Cited by 124
Response to Rv2628 latency antigen associates with cured tuberculosis and remote infection
Goletti, D., Butera, O., Vanini, V., Lauria, F., Lange, C. G., Franken, K. L. M. C., Angeletti, C., Ottenhoff, T. H. M., & Girardi, E. (2009) · European Respiratory Journal · doi:10.1183/09031936.00140009 · Cited by 122
Stevanin, T. M., MOIR, J. W. B., & Read, R. C. (2005) · Infection and Immunity · doi:10.1128/iai.73.6.3322-3329.2005 · Cited by 124
Mak, P. A., Rao, S. P. S., Tan, M. P., Lin, X., Chyba, J., Tay, J. A., Ng, S. H., Tan, B. H., Cherian, J., Duraiswamy, J., et al. (2012) · ACS Chemical Biology · doi:10.1021/cb2004884 · Cited by 121
The PE and PPE proteins of Mycobacterium tuberculosis
Mukhopadhyay, S., & Balaji, K. N. (2011) · Tuberculosis · doi:10.1016/j.tube.2011.04.004 · Cited by 123
Rodríguez, J. G., Hernández, A. C., Helguera‐Repetto, A. C., Aguilar-Ayala, D. A., Guadarrama-Medina, R., Anzola, J. M., Bustos, J. R., Zambrano, M. M., González-y-Merchand, J. A., García, M. J., et al. (2014) · mBio · doi:10.1128/mbio.01125-14 · Cited by 124
Zimmermann, M., Zimmermann‐Kogadeeva, M., Gengenbacher, M., McEwen, G. K., Mollenkopf, H., Zamboni, N., Kaufmann, S. H. E., & Sauer, U. (2017) · mSystems · doi:10.1128/msystems.00057-17 · Cited by 120
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Bowman, L. A. H., McLean, S., Poole, R. K., & Fukuto, J. M. (2011) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/b978-0-12-387661-4.00006-9 · Cited by 118
Schnell, R., Sandalova, T., Hellman, U., Lindqvist, Y., & Schneider, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502560200 · Cited by 117
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Zhang, Y. J., & Rubin, E. J. (2013) · Cellular Microbiology · doi:10.1111/cmi.12140 · Cited by 117
Tian, J., Bryk, R., Shi, S., Erdjument‐Bromage, H., Tempst, P., & Nathan, C. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04741.x · Cited by 117
Self-citationWaddell, S. J., Stabler, R. A., Laing, K. G., Kremer, L., Reynolds, R. C., & Besra, G. S. (2004) · Tuberculosis · doi:10.1016/j.tube.2003.12.005 · Cited by 115
Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase
Chauhan, A., Lofton, H., Maloney, E., Moore, J., Fol, M., Madiraju, M. V. V. S., & Rajagopalan, M. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05333.x · Cited by 116
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Chen, C., Gardete, S., Jansen, R. S., Shetty, A., Dick, T., Rhee, K. Y., & Dartois, V. A. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02107-17 · Cited by 117
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Andersen, P. L. (2006) · Trends in Microbiology · doi:10.1016/j.tim.2006.11.008 · Cited by 116
Pang, X., Vu, P., Byrd, T. F., Ghanny, S., Soteropoulos, P., Mukamolova, G. V., Wu, S., Samten, B., & Howard, S. T. (2007) · Microbiology · doi:10.1099/mic.0.29281-0 · Cited by 115
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Co, D. O., Hogan, L. H., Kim, S., & Sándor, M. (2004) · Clinical Immunology · doi:10.1016/j.clim.2004.08.012 · Cited by 114
Differential network expression during drug and stress response
Cabusora, L., Sutton, E., Fulmer, A. W., & Forst, C. V. (2005) · Computer applications in the biosciences · doi:10.1093/bioinformatics/bti440 · Cited by 114
Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids
Gokhale, R. S., Saxena, P., Chopra, T., & Mohanty, D. (2007) · Natural Product Reports · doi:10.1039/b616817p · Cited by 114
Singh, P., Rao, R. N., Reddy, J. R. C., Prasad, R., Kotturu, S. K., Ghosh, S., & Mukhopadhyay, S. (2016) · Scientific Reports · doi:10.1038/srep21624 · Cited by 114
Pasqua, M., Grossi, M., Zennaro, A., Fanelli, G., Micheli, G., Barras, F., Colonna, B., & Prosseda, G. (2019) · Microorganisms · doi:10.3390/microorganisms7090285 · Cited by 111
Bansal, K., Elluru, S. R., Yeddula, N., Chaturvedi, R., Patil, S. A., Kaveri, S. V., Bayry, J., & Balaji, K. N. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903299 · Cited by 113
Senaratne, R. H., Silva, A. D. D., Williams, S. J., Mougous, J. D., Reader, J. R., Zhang, T., Chan, S., Sidders, B. S., Lee, D. H., Chan, J., et al. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05075.x · Cited by 113
Dodecameric Structure of the Small Heat Shock Protein Acr1 from Mycobacterium tuberculosis
Kennaway, C. K., Benesch, J. L. P., Gohlke, U., Wang, L., Robinson, C. V., Orlova, E. V., Saibi, H. R., & Keep, N. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504263200 · Cited by 113
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Hatzios, S. K., & Bertozzi, C. R. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002036 · Cited by 114
Non-coding RNA and its potential role in Mycobacterium tuberculosis pathogenesis
Arnvig, K. B., & Young, D. B. (2012) · RNA Biology · doi:10.4161/rna.20105 · Cited by 113
Lack, N. A., Yam, K. C., Lowe, E. D., Horsman, G. P., Owen, R. L., Sim, E., & Eltis, L. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.058081 · Cited by 110
Common Variants in the Glycerol Kinase Gene Reduce Tuberculosis Drug Efficacy
Bellerose, M. M., Baek, S.-H., Huang, C., Moss, C. E., Koh, E., Proulx, M. K., Smith, C. M., Baker, R. E., Lee, J. S., Eum, S., et al. (2019) · mBio · doi:10.1128/mbio.00663-19 · Cited by 110
Bansal, K., Sinha, A. Y., Ghorpade, D. S., Togarsimalemath, S. K., Patil, S. A., Kaveri, S. V., Balaji, K. N., & Bayry, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.158055 · Cited by 109
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Marrero, J., Trujillo, C., Rhee, K. Y., & Ehrt, S. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003116 · Cited by 108
Self-citationSchnell, R., Oehlmann, W., Singh, M., & Schneider, G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703518200 · Cited by 108
Gold, B. S., Pingle, M., Brickner, S. J., Shah, N., Roberts, J., Rundell, M. S., Bracken, W. C., Warrier, T., Somersan, S., Venugopal, A., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214188109 · Cited by 107
Self-citationMycobacterium tuberculosis Complex Members Adapted to Wild and Domestic Animals
Malone, K. M., & Gordon, S. V. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-64371-7_7 · Cited by 115
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Shi, S., & Ehrt, S. (2005) · Infection and Immunity · doi:10.1128/iai.74.1.56-63.2006 · Cited by 107
Self-citationJung, J., Madan-Lala, R., Georgieva, M., Rengarajan, J., Sohaskey, C. D., Bange, F., & Robinson, C. M. (2013) · Infection and Immunity · doi:10.1128/iai.00611-13 · Cited by 110
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Warner, D. F. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a021121 · Cited by 108
Alteri, C. J., Himpsl, S. D., & Mobley, H. L. T. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004601 · Cited by 100
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Soldati, T., & Neyrolles, O. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01358.x · Cited by 111
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Yang, X., Nesbitt, N. M., Dubnau, E., Smith, I., & Sampson, N. S. (2009) · Biochemistry · doi:10.1021/bi9005418 · Cited by 107
Singh, A., Gupta, R., Vishwakarma, R. A., Narayanan, P. R., Paramasivan, C. N., Ramanathan, V. D., & Tyagi, A. K. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.12.4173-4186.2005 · Cited by 105
Lin, M. Y., Geluk, A., Smith, S. G., Stewart, A. L., Friggen, A. H., Franken, K. L. M. C., Verduyn, M. J. C., van Meijgaarden, K. E., Voskuil, M. I., Dockrell, H. M., et al. (2007) · Infection and Immunity · doi:10.1128/iai.01999-06 · Cited by 105
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Billig, S., Schneefeld, M., Huber, C., Graßl, G. A., Eisenreich, W., & Bange, F. (2017) · Scientific Reports · doi:10.1038/s41598-017-05916-7 · Cited by 104
Dutta, N. K., Mehra, S., & Kaushal, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010069 · Cited by 103
Hit Generation in TB Drug Discovery: From Genome to Granuloma
Yuan, T., & Sampson, N. S. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00602 · Cited by 104
Pullen, K. E., Ng, H. L., Sung, P.-Y., Good, M. C., Smith, S. M., & Alber, T. (2004) · Structure · doi:10.1016/j.str.2004.09.008 · Cited by 105
Laval, T., Chaumont, L., & Demangel, C. (2021) · Immunological Reviews · doi:10.1111/imr.12952 · Cited by 103
Tan, M. P., de Sequeira, P. C., Lin, W. W., Phong, W. Y., Cliff, P. R., Ng, S. H., Lee, B. H., Camacho, L. R., Schnappinger, D., Ehrt, S., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013356 · Cited by 99
Self-citationRogerson, B. J., Jung, Y., LaCourse, R., Ryan, L., Enright, N., & North, R. J. (2006) · Immunology · doi:10.1111/j.1365-2567.2006.02355.x · Cited by 101
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Kusner, D. J. (2004) · Clinical Immunology · doi:10.1016/j.clim.2004.07.016 · Cited by 103
Johnston, J. B., Ouellet, H., & de Montellano, P. R. O. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.161117 · Cited by 101
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Silva, M. T., Portaels, F., & Pedrosa, J. (2009) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(09)70234-8 · Cited by 113
Role of cholesterol in Mycobacterium tuberculosis infection.
Miner, M. D., Chang, J. C., Pandey, A. K., Sassetti, C. M., & Sherman, D. R. (2009) · PubMed · Cited by 101
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Esmail, H., Barry, C. E., & Wilkinson, R. J. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.12.013 · Cited by 97
Cunningham‐Bussel, A., Zhang, T., & Nathan, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316894110 · Cited by 98
Self-citationRienksma, R. A., Diez, M. S., Mollenkopf, H., Dolganov, G., Dorhoi, A., Schoolnik, G. K., dos Santos, V. A. P. M., Kaufmann, S. H. E., Schaap, P. J., & Gengenbacher, M. (2015) · BMC Genomics · doi:10.1186/s12864-014-1197-2 · Cited by 100
Self-citationChawla, M., Parikh, P., Saxena, A., Munshi, M., Mehta, M., Mai, D., Srivastava, A. K., Narasimhulu, K. V., Redding, K., Vashi, N., et al. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08165.x · Cited by 101
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Chang, J. C., Harik, N., Liao, R., & Sherman, D. R. (2007) · The Journal of Infectious Diseases · doi:10.1086/520089 · Cited by 100
Talaat, A. M., Ward, S. K., Wu, C., Rondon, E., Tavano, C. L., Bannantine, J. P., Lyons, R., & Johnston, S. A. (2007) · Journal of Bacteriology · doi:10.1128/jb.00011-07 · Cited by 98
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Hards, K., & Cook, G. M. (2017) · Drug Resistance Updates · doi:10.1016/j.drup.2017.11.001 · Cited by 102
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Flores, L., Steingart, K. R., Dendukuri, N., Schiller, I., Minion, J., Pai, M., Ramsay, A., Henry, M., & Laal, S. (2011) · Clinical and Vaccine Immunology · doi:10.1128/cvi.05205-11 · Cited by 99
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Mehta, M., Rajmani, R. S., & Singh, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.684597 · Cited by 98
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Hoang, T. T. K. T., Aagaard, C., Dietrich, J., Cassidy, J. P., Dolganov, G., Schoolnik, G. K., Lundberg, C. V., Agger, E. M., & Andersen, P. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080579 · Cited by 95
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Ouellet, H., Johnston, J. B., & de Montellano, P. R. O. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.07.011 · Cited by 98
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Movahedzadeh, F., Smith, D. A., Norman, R. A., Dinadayala, P., Murray‐Rust, J., Russell, D. G., Kendall, S. L., Rison, S. C. G., McAlister, M. S. B., Bancroft, G. J., et al. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03900.x · Cited by 96
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Casali, N., White, A. M., & Riley, L. W. (2005) · Journal of Bacteriology · doi:10.1128/jb.188.2.441-449.2006 · Cited by 96
Subbian, S., Tsenova, L., O’Brien, P. E., Yang, G., Koo, M.-S., Peixoto, B., Fallows, D. A., Dartois, V. A., Muller, G. W., & Kaplan, G. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002262 · Cited by 94
Mehra, S., & Kaushal, D. (2009) · Journal of Bacteriology · doi:10.1128/jb.00064-09 · Cited by 95
Meibom, K. L., Dubail, I., Dupuis, M., Barel, M., Lenčo, J., Stulík, J., Golovliov, I. R., Sjöstedt, A. B., & Charbit, A. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06139.x · Cited by 95
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Cappelli, G., Volpe, E., Grassi, M., Liseo, B., Colizzi, V., & Mariani, F. (2006) · Research in Microbiology · doi:10.1016/j.resmic.2005.10.007 · Cited by 94
Charlet, D., Mostowy, S., Alexander, D. C., Sit, L., Wiker, H. G., & Behr, M. A. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04618.x · Cited by 93
Fivian-Hughes, A. S., Houghton, J., & Davis, E. O. (2011) · Microbiology · doi:10.1099/mic.0.053983-0 · Cited by 93
Capyk, J. K., Casabon, I., Gruninger, R. J., Strynadka, N. C. J., & Eltis, L. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.289975 · Cited by 92
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Richardson, E. T., Shukla, S., Sweet, D. R., Wearsch, P. A., Tsichlis, P. N., Boom, W. H., & Harding, C. V. (2015) · Infection and Immunity · doi:10.1128/iai.00135-15 · Cited by 91
Chen, Z., Hu, Y., Cumming, B. M., Lu, P., Feng, L., Deng, J., Steyn, A. J. C., & Chen, S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.080 · Cited by 95
Manganelli, R., Fattorini, L., Tan, D., Iona, E., Orefici, G., Altavilla, G., Cusatelli, P., & Smith, I. (2004) · Infection and Immunity · doi:10.1128/iai.72.5.3038-3041.2004 · Cited by 91
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Honaker, R. W., Dhiman, R. K., Narayanasamy, P., Crick, D. C., & Voskuil, M. I. (2010) · Journal of Bacteriology · doi:10.1128/jb.00978-10 · Cited by 87
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Martino, A., Badell, E., Abadie, V., Balloy, V., Chignard, M., Mistou, M., Combadière, B., Combadière, C., & Winter, N. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903348 · Cited by 86
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Stapleton, M. R., Haq, I., Hunt, D. M., Arnvig, K. B., Artymiuk, P. J., Buxton, R. S., & Green, J. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.047720 · Cited by 86
Bacon, J., Dover, L. G., Hatch, K. A., Zhang, Y., Gomes, J. M., Kendall, S. L., Wernisch, L., Stoker, N. G., Butcher, P. D., Besra, G. S., et al. (2007) · Microbiology · doi:10.1099/mic.0.2006/004317-0 · Cited by 87
Self-citationPang, X., Samten, B., Cao, G., Wang, X., Tvinnereim, A., Chen, X.-L., & Howard, S. T. (2012) · Journal of Bacteriology · doi:10.1128/jb.01067-12 · Cited by 80
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Metadata
- Authors
- Schnappinger, D., Ehrt, S., Voskuil, M. I., Liu, Y., Mangan, J. A., Monahan, I. M., Dolganov, G., Efron, B., Butcher, P. D., Nathan, C., & Schoolnik, G. K.
- Affiliations
- Cornell University (US)
- 3Department of Microbiology and Immunology, Weill Medical College and Graduate Programs in
- Stanford Medicine (US)
- St George's, University of London (GB)
- University of California, San Francisco (US)
- Stanford University (US)
- Corresponding author
- Schnappinger, Dirk
- ORCID
- Venue
- The Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2003-09-01
- Volume
- 198
- Issue
- 5
- Pages
- 693-704
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2194186
- OpenAlex
- W2007097682
- Cited by
- 1,420
- References
- 58
- Citations by year
- 2026: 26 · 2025: 35 · 2024: 46 · 2023: 32 · 2022: 55 · 2021: 41 · 2020: 37 · 2019: 68 · 2018: 63 · 2017: 65 · 2016: 61 · 2015: 96 · 2014: 90 · 2013: 75 · 2012: 96
- FWCI
- 31.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- St George's Online Research Archive (St George's University of London) (acceptedVersion)
- Funders
- Hearst Foundations
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- Defense Advanced Research Projects Agency
- Advanced Research Projects Agency
- Medical Research Council
- National Heart, Lung, and Blood Institute (R01HL068525, HL 61241, HL68525, R01HL061241)
- National Institute of Allergy and Infectious Diseases (R01AI044826, AI-44826)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Mycobacterium tuberculosis, macrophages, nitric oxide synthase 2, interferon-gamma, iron scavenging, anaerobic respiration, fatty acid beta-oxidation, sigma E, cell envelope damage, hypoxia, nitrosative stress, tuberculosis pathogenesis
- MeSH terms
- Animals, Macrophages, Mycobacterium tuberculosis, Phagosomes, RNA, Bacterial, Transcription, Genetic, Gene Expression Regulation, Bacterial, Mice
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