Mechanisms of iron regulation in mycobacteria: role in physiology and virulence

Rodriguez, G. Marcela; Smith, Issar

doi:10.1046/j.1365-2958.2003.03384.x

Cited by 163Tuberculosis Research and EpidemiologyBacterial Genetics and BiotechnologyIron Metabolism and Disorders

Mechanisms of iron regulation in mycobacteria: role in physiology and virulence

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Rodriguez, G. Marcela, Smith, Issar·2003·Molecular Microbiology

DOI 10.1046/j.1365-2958.2003.03384.x

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Abstract

Summary: The role of iron in mycobacteria as in other bacteria goes beyond the need for this essential cofactor. Limitation of this metal triggers an extensive response aimed at increasing iron acquisition while coping with iron deficiency. In contrast, iron‐rich environments prompt these prokaryotes to induce synthesis of iron storage molecules and to increase mechanisms of protection against iron‐mediated oxidative damage. The response to changes in iron availability is strictly regulated in order to maintain sufficient but not excessive and potentially toxic levels of iron in the cell. This response is also linked to other important processes such as protection against oxidative stress and virulence. In bacteria, iron metabolism is regulated by controlling transcription of genes involved in iron uptake, transport and storage. In mycobacteria, this role is fulfilled by the i ron‐d ependent r egulator IdeR. IdeR is an essential protein in Mycobacterium tuberculosis, the causative agent of human tuberculosis. It functions as a repressor of iron acquisition genes, but is also an activator of iron storage genes and a positive regulator of oxidative stress responses.

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In Fe-replete conditions, two IdeR homodimers with four bound Fe ions recognize a 19-base-pair palindromic sequence and negatively regulate expression of proteins required in Fe-depleted conditions.
“Two homodimers with four bound Fe ions recognize a 19-base-pair palindromic sequence and in Fe-replete conditions and negatively regulate the expression of proteins required in Fe-depleted conditions [65].”
From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [65]

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Iron and microbial infection
Schaible, U. E., & Kaufmann, S. H. E. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1046 · Cited by 945 · see citing works
Type VII secretion — mycobacteria show the way
Abdallah, A. M., Gey van Pittius, N. C., DiGiuseppe Champion, P. A., Cox, J., Luirink, J., Vandenbroucke-Grauls, C. M. J. E., Appelmelk, B. J., & Bitter, W. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1773 · Cited by 763 · see citing works
Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
Elemental Analysis of Mycobacterium avium -, Mycobacterium tuberculosis -, and Mycobacterium smegmatis -Containing Phagosomes Indicates Pathogen-Induced Microenvironments within the Host Cell’s Endosomal System
Wagner, D., Maser, J. M., Lai, B. C. H., Cai, Z., Barry, C. E., zu Bentrup, K. H., Russell, D. G., & Bermudez, L. E. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.3.1491 · Cited by 430 · see citing works
THE MAGIC BULLETS AND TUBERCULOSIS DRUG TARGETS
Zhang, Y. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.100120 · Cited by 432 · see citing works
Carbon metabolism of intracellular bacteria
Muñoz‐Elías, E. J., & McKinney, J. D. (2005) · Cellular Microbiology · doi:10.1111/j.1462-5822.2005.00648.x · Cited by 266 · see citing works
pkn22 (alr2502) encoding a putative Ser/Thr kinase in the cyanobacterium Anabaena sp. PCC 7120 is induced by both iron starvation and oxidative stress and regulates the expression of isiA
Xu, W., Jeanjean, R., Liu, Y., & Zhang, C. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01019-6 · Cited by 230 · see citing works
The σ factors ofMycobacterium tuberculosis
Rodrigue, S., Provvedi, R., Jacques, P., Gaudreau, L. R., & Manganelli, R. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00040.x · Cited by 228 · see citing works
Mycobacteria, metals, and the macrophage
Neyrolles, O., Wolschendorf, F., Mitra, A., & Niederweis, M. (2015) · Immunological Reviews · doi:10.1111/imr.12265 · Cited by 217 · see citing works
Identification of a copper-binding metallothionein in pathogenic mycobacteria
Gold, B., Deng, H., Bryk, R., Vargas, D., Eliezer, D., Roberts, J., Jiang, X., & Nathan, C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.109 · Cited by 217 · see citing works
σ Factors and Global Gene Regulation inMycobacterium tuberculosis
Manganelli, R., Provvedi, R., Rodrigue, S., Beaucher, J., Gaudreau, L. R., & Smith, I. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.4.895-902.2004 · Cited by 215 · see citing works
Self-citation
Characterization of aMycobacterium tuberculosisESX-3 Conditional Mutant: Essentiality and Rescue by Iron and Zinc
Serafini, A., Boldrin, F., Palù, G., & Manganelli, R. (2009) · Journal of Bacteriology · doi:10.1128/jb.00756-09 · Cited by 198 · see citing works
Virulence factors and their mechanisms of action: the view from a damage–response framework
Casadevall, A., & Pirofski, L. (2009) · Journal of Water and Health · doi:10.2166/wh.2009.036 · Cited by 191 · see citing works
Lipoproteins ofMycobacterium tuberculosis: an abundant and functionally diverse class of cell envelope components
Sutcliffe, I. C., & Harrington, D. J. (2004) · FEMS Microbiology Reviews · doi:10.1016/j.femsre.2004.06.002 · Cited by 183 · see citing works
Oxygen status of lung granulomas in Mycobacterium tuberculosis‐infected mice
Aly, S., Wagner, K. F., Keller, C., Malm, S., Malzan, A., Brandau, S., Bange, F. C., & Ehlers, S. (2006) · The Journal of Pathology · doi:10.1002/path.2055 · Cited by 184 · see citing works
A Ferroxidation/Permeation Iron Uptake System Is Required for Virulence inUstilago maydis
Eichhorn, H., Leßing, F., Winterberg, B., Schirawski, J., Kämper, J., Müller, P., & Kahmann, R. (2006) · The Plant Cell · doi:10.1105/tpc.106.043588 · Cited by 167 · see citing works
Unraveling the Secret Lives of Bacteria: Use of In Vivo Expression Technology and Differential Fluorescence Induction Promoter Traps as Tools for Exploring Niche-Specific Gene Expression
Rediers, H., Rainey, P. B., Vanderleyden, J., & Mot, R. D. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.2.217-261.2005 · Cited by 157 · see citing works
Identification of theMycobacterium tuberculosisSUF Machinery as the Exclusive Mycobacterial System of [Fe-S] Cluster Assembly: Evidence for Its Implication in the Pathogen's Survival
Huet, G., Daffé, M., & Saves, I. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.17.6137-6146.2005 · Cited by 156 · see citing works
The role of iron in Mycobacterium smegmatis biofilm formation: the exochelin siderophore is essential in limiting iron conditions for biofilm formation but not for planktonic growth
Ojha, A. K., & Hatfull, G. F. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05935.x · Cited by 149 · see citing works
Crystal Structure and Function of the Zinc Uptake Regulator FurB from Mycobacterium tuberculosis
Lucarelli, D., Russo, S., Garman, E. F., Milano, A., Meyer‐Klaucke, W., & Pohl, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609974200 · Cited by 144 · see citing works
Targeting Phenotypically Tolerant Mycobacterium tuberculosis
Gold, B. S., & Nathan, C. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.tbtb2-0031-2016 · Cited by 132 · see citing works
A genetic locus required for iron acquisition in Mycobacterium tuberculosis
Krithika, R., Marathe, U., Saxena, P., Ansari, M. Z., Mohanty, D., & Gokhale, R. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507924103 · Cited by 129 · see citing works
Whole genome identification of Mycobacterium tuberculosisvaccine candidates by comprehensive data mining and bioinformatic analyses
Zvi, A., Ariel, N., Fulkerson, J., SADOFF, J. C., & Avigdor Shafferman, C. (2008) · BMC Medical Genomics · doi:10.1186/1755-8794-1-18 · Cited by 129 · see citing works
Disruption of Mycobactin Biosynthesis Leads to Attenuation of Mycobacterium tuberculosis for Growth and Virulence
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 · see citing works
Iron Storage Proteins Are Essential for the Survival and Pathogenesis of Mycobacterium tuberculosis in THP-1 Macrophages and the Guinea Pig Model of Infection
Reddy, P. V., Puri, R. V., Khera, A., & Tyagi, A. K. (2011) · Journal of Bacteriology · doi:10.1128/jb.05553-11 · Cited by 125 · see citing works
Reconsidering Adjuvant Immunotherapy for Tuberculosis
Wallis, R. S. (2005) · Clinical Infectious Diseases · doi:10.1086/430914 · Cited by 121 · see citing works
Identification of Francisella tularensis Genes Affected by Iron Limitation
Deng, K., Blick, R. J., Liu, W. Y., & Hansen, E. J. (2006) · Infection and Immunity · doi:10.1128/iai.01975-05 · Cited by 114 · see citing works
The Regulation of Sulfur Metabolism in Mycobacterium tuberculosis
Hatzios, S. K., & Bertozzi, C. R. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002036 · Cited by 112 · see citing works
The AraC-type Regulator RipA Represses Aconitase and Other Iron Proteins from Corynebacterium under Iron Limitation and Is Itself Repressed by DtxR
Frunzke, J., Krug, A., & Bott, M. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508693200 · Cited by 111 · see citing works
No effects without causes: the Iron Dysregulation and Dormant Microbes hypothesis for chronic, inflammatory diseases
Kell, D. B., & Pretorius, E. (2018) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12407 · Cited by 113 · see citing works
Iron and infection: effects of host iron status and the iron-regulatory genes haptoglobin and NRAMP1 (SLC11A1) on host–pathogen interactions in tuberculosis and HIV
McDermid, J. M., & Prentice, A. M. (2006) · Clinical Science · doi:10.1042/cs20050273 · Cited by 102 · see citing works
The Structure of MbtI from Mycobacterium tuberculosis , the First Enzyme in the Biosynthesis of the Siderophore Mycobactin, Reveals It To Be a Salicylate Synthase
Harrison, A. J., Yu, M., Gårdenborg, T., Middleditch, M., Ramsay, R. J., Baker, E. N., & Lott, J. S. (2006) · Journal of Bacteriology · doi:10.1128/jb.00338-06 · Cited by 102 · see citing works
The Nickel-Responsive Regulator NikR Controls Activation and Repression of Gene Transcription inHelicobacter pylori
Ernst, F. D., Kuipers, E. J., Heijens, A., Sarwari, R., Stoof, J., Penn, C. W., Kusters, J. G., & van Vliet, A. H. M. (2005) · Infection and Immunity · doi:10.1128/iai.73.11.7252-7258.2005 · Cited by 101 · see citing works
Microarray analysis and redox control of gene expression in the cyanobacterium Synechocystis sp. PCC 6803
Singh, A. K., Li, H., & Sherman, L. A. (2004) · Physiologia Plantarum · doi:10.1111/j.0031-9317.2004.0232.x · Cited by 86 · see citing works
Lipid composition and transcriptional response of Mycobacterium tuberculosis grown under iron-limitation in continuous culture: identification of a novel wax ester
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 · see citing works
What do microarrays really tell us about M. tuberculosis?
Kendall, S. L., Rison, S. C. G., Movahedzadeh, F., Frita, R., & Stoker, N. G. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.10.005 · Cited by 81 · see citing works
TheMycobacterium tuberculosisSigma Factor σBIs Required for Full Response to Cell Envelope Stress and Hypoxia In Vitro, but It Is Dispensable for In Vivo Growth
Fontán, P. A., Voskuil, M. I., Gómez, M. J., Tan, D., Pardini, M., Manganelli, R., Fattorini, L., Schoolnik, G. K., & Smith, I. (2009) · Journal of Bacteriology · doi:10.1128/jb.00510-09 · Cited by 79 · see citing works
Self-citation
The global transcriptional response of Bacillus subtilis to manganese involves the MntR, Fur, TnrA and σB regulons
Guédon, E., Moore, C. M., Que, Q. Q., Wang, T., Ye, R. W., & Helmann, J. D. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03648.x · Cited by 80 · see citing works
Structure elucidation and biosynthesis of fuscachelins, peptide siderophores from the moderate thermophile Thermobifida fusca
Dimise, E. J., Widboom, P. F., & Bruner, S. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805451105 · Cited by 77 · see citing works
The complex architecture of mycobacterial promoters
Newton-Foot, M., & van Pittius, N. C. G. (2012) · Tuberculosis · doi:10.1016/j.tube.2012.08.003 · Cited by 74 · see citing works
Iron Metabolism: A Promising Target for Antibacterial Strategies
Ballouche, M., Cornélis, P., & Baysse, C. (2009) · Recent Patents on Anti-Infective Drug Discovery · doi:10.2174/157489109789318514 · Cited by 76 · see citing works
Iron and iron chelating agents modulateMycobacterium tuberculosisgrowth and monocyte-macrophage viability and effector functions
Cronjé, L., Edmondson, N., Eisenach, K. D., & Bornman, L. (2005) · FEMS Immunology & Medical Microbiology · doi:10.1016/j.femsim.2005.02.007 · Cited by 72 · see citing works
Leprosy pathogenetic background: a review and lessons from other mycobacterial diseases
Goulart, L. R., & Goulart, I. M. B. (2008) · Archives of Dermatological Research · doi:10.1007/s00403-008-0917-3 · Cited by 71 · see citing works
Pathogenesis in tuberculosis: transcriptomic approaches to unraveling virulence mechanisms and finding new drug targets
Mukhopadhyay, S., Nair, S., & Ghosh, S. (2011) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2011.00302.x · Cited by 67 · see citing works
Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality?
Kopeckova, M., Pávková, I., & Stulík, J. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00089 · Cited by 63 · see citing works
M. tuberculosis intramembrane protease Rip1 controls transcription through three anti‐sigma factor substrates
Sklar, J. G., Makinoshima, H., Schneider, J. S., & Glickman, M. S. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07232.x · Cited by 63 · see citing works
Ferritin Structure from Mycobacterium tuberculosis: Comparative Study with Homologues Identifies Extended C-Terminus Involved in Ferroxidase Activity
Khare, G., Gupta, V., Nangpal, P., Gupta, R. K., Sauter, N. K., & Tyagi, A. K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018570 · Cited by 62 · see citing works
Individuality, phenotypic differentiation, dormancy and ‘persistence’ in culturable bacterial systems: commonalities shared by environmental, laboratory, and clinical microbiology
Kell, D. B., Potgieter, M., & Pretorius, E. (2015) · F1000Research · doi:10.12688/f1000research.6709.2 · Cited by 58 · see citing works
Mechanistic Insights into a Novel Exporter-Importer System of Mycobacterium tuberculosis Unravel Its Role in Trafficking of Iron
Farhana, A., Kumar, S., Rathore, S. S., Ghosh, P. C., Ehtesham, N. Z., Tyagi, A. K., & Hasnain, S. E. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002087 · Cited by 60 · see citing works
Iron enhances the antituberculous activity of pyrazinamide
Somoskövi, Á. (2004) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkh042 · Cited by 58 · see citing works
Pathogenic Mycobacteria
Rodríguez, G. M., & Smith, I. (2014) · ASM Press eBooks · doi:10.1128/9781555816544.ch23 · Cited by 57 · see citing works
Self-citation
Involvement of Fumarase C and NADH Oxidase in Metabolic Adaptation of Pseudomonas fluorescens Cells Evoked by Aluminum and Gallium Toxicity
Chénier, D., Bériault, R., Mailloux, R., Baquié, M., Abramia, G., Lemire, J., & Appanna, V. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.02702-07 · Cited by 55 · see citing works
Strategies of intracellular pathogens for obtaining iron from the environment
Leon-Sicairos, N., Reyes-Cortes, R., Guadrón-Llanos, A. M., Madueña-Molina, J., Leon-Sicairos, C., & Canizalez-Román, A. (2015) · BioMed Research International · doi:10.1155/2015/476534 · Cited by 51 · see citing works
“Two homodimers with four bound Fe ions recognize a 19-base-pair palindromic sequence and in Fe-replete conditions and negatively regulate the expression of proteins required in Fe-depleted conditions [65].”
Background
Host-pathogen redox dynamics modulate Mycobacterium tuberculosis pathogenesis
Pacl, H. T., Reddy, V. P., Saini, V., Chinta, K. C., & Steyn, A. J. C. (2018) · Pathogens and Disease · doi:10.1093/femspd/fty036 · Cited by 51 · see citing works
Ultrastructural Analysis of Cell Envelope and Accumulation of Lipid Inclusions in Clinical Mycobacterium tuberculosis Isolates from Sputum, Oxidative Stress, and Iron Deficiency
Vijay, S., Hai, H. T., Thu, D. D. A., Johnson, E., Pielach, A., Phu, N. H., Thwaites, G. E., & Thương, N. T. T. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02681 · Cited by 49 · see citing works
Regulation of Three Virulence Strategies of Mycobacterium tuberculosis: A Success Story
Zondervan, N. A., van Dam, J. C. J., Schaap, P. J., dos Santos, V. A. P. M., & Diez, M. S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020347 · Cited by 48 · see citing works
The Nature of Extracellular Iron Influences Iron Acquisition by Mycobacterium tuberculosis Residing within Human Macrophages
Olakanmi, O., Schlesinger, L., Ahmed, A., & Britigan, B. (2004) · Infection and Immunity · doi:10.1128/iai.72.4.2022-2028.2004 · Cited by 48 · see citing works
Two overlapping antiparallel genes encoding the iron regulator DmdR1 and the Adm proteins control sidephore and antibiotic biosynthesis in Streptomyces coelicolor A3(2)
Tunca, S., Barreiro, C., Coque, J. J. R., & Martin, J. F. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07182.x · Cited by 47 · see citing works
Identification of a promoter motif regulating the major DNA damage response mechanism ofMycobacterium tuberculosis
Gamulin, V., Ćetković, H., & Ahel, I. (2004) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2004.tb09737.x · Cited by 47 · see citing works
Contrasting Transcriptional Responses of a Virulent and an Attenuated Strain of Mycobacterium tuberculosis Infecting Macrophages
Li, A. H., Waddell, S. J., Hinds, J., Malloff, C. A., Bains, M., Hancock, R. E. W., Lam, W. L., Butcher, P. D., & Stokes, R. W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011066 · Cited by 47 · see citing works
A 38-Kilobase Pathogenicity Island Specific forMycobacterium aviumsubsp.paratuberculosisEncodes Cell Surface Proteins Expressed in the Host
Stratmann, J., Strommenger, B., Goethe, R., Dohmann, K., Gerlach, G.-F., Stevenson, K., Li, L.-L., Zhang, Q., Kapur, V., & Bull, T. J. (2004) · Infection and Immunity · doi:10.1128/iai.72.3.1265-1274.2004 · Cited by 45 · see citing works
Computational prediction and experimental verification of novel IdeR binding sites in the upstream sequences of Mycobacterium tuberculosis open reading frames
Prakash, P., Yellaboina, S., Ranjan, A., & Hasnain, S. E. (2005) · Computer applications in the biosciences · doi:10.1093/bioinformatics/bti375 · Cited by 45 · see citing works
Transcriptional profiling of Mycoplasma hyopneumoniae during iron depletion using microarrays
Madsen, M. L., Nettleton, D. S., Thacker, E. L., & Minion, F. C. (2006) · Microbiology · doi:10.1099/mic.0.28674-0 · Cited by 45 · see citing works
Crystal Structure of Bfr A from Mycobacterium tuberculosis: Incorporation of Selenomethionine Results in Cleavage and Demetallation of Haem
Gupta, V., Gupta, R. K., Khare, G., Salunke, D. M., & Tyagi, A. K. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008028 · Cited by 44 · see citing works
Crystal Structures, Metal Activation, and DNA-Binding Properties of Two-Domain IdeR from Mycobacterium tuberculosis,
Wisedchaisri, G., Chou, C. J., Wu, M., Roach, C., Rice, A. E., Holmes, R. K., Beeson, C. C., & Hol, W. G. J. (2006) · Biochemistry · doi:10.1021/bi0609826 · Cited by 44 · see citing works
Mechanism of Iron Ion Homeostasis in Intestinal Immunity and Gut Microbiota Remodeling
Bao, H., Wang, Y., Xiong, H., Xia, Y., Cui, Z., & Liu, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020727 · Cited by 47 · see citing works
Host-Mycobacterium avium subsp. paratuberculosis interactome reveals a novel iron assimilation mechanism linked to nitric oxide stress during early infection
Lamont, E. A., Xu, W. W., & Sreevatsan, S. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-694 · Cited by 40 · see citing works
Mycobacterium tuberculosis NmtR Harbors a Nickel Sensing Site with Parallels to Escherichia coli RcnR
Reyes-Caballero, H., Lee, C. W., & Giedroc, D. P. (2011) · Biochemistry · doi:10.1021/bi200737a · Cited by 39 · see citing works
MtsR is a dual regulator that controls virulence genes and metabolic functions in addition to metal homeostasis in the group A streptococcus
Toukoki, C., Gold, K. M., McIver, K. S., & Eichenbaum, Z. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07157.x · Cited by 37 · see citing works
Identification and functional characterization of the iron-dependent regulator (IdeR) of Mycobacterium avium subsp. paratuberculosis
Janagama, H. K., Senthilkumar, T. M. A., Bannantine, J. P., Rodríguez, G. M., Smith, I., Paustian, M. L., McGarvey, J. A., & Sreevatsan, S. (2009) · Microbiology · doi:10.1099/mic.0.031948-0 · Cited by 39 · see citing works
Self-citation
Proteases in Mycobacterium Tuberculosis Pathogenesis: Potential as Drug Targets
Roberts, D. M., Personne, Y., Ollinger, J., & Parish, T. (2013) · Future Microbiology · doi:10.2217/fmb.13.25 · Cited by 39 · see citing works
Mycobacterial extracellular vesicles and host pathogen interactions
Gupta, S., & Rodríguez, G. M. (2018) · Pathogens and Disease · doi:10.1093/femspd/fty031 · Cited by 34 · see citing works
Metalloregulators: Arbiters of Metal Sufficiency
Helmann, J. D., Soonsanga, S., & Gabriel, S. E. (2007) · Springer eBooks · doi:10.1007/7171_2006_073 · Cited by 33 · see citing works
Identification and Characterization of a Major Cell Wall-Associated Iron-Regulated Envelope Protein (Irep-28) in Mycobacterium tuberculosis
Yeruva, C. V., Duggirala, S., Lakshmi, V., Kolarich, D., Altmann, F., & Sritharan, M. (2006) · Clinical and Vaccine Immunology · doi:10.1128/cvi.00125-06 · Cited by 34 · see citing works
Protein Dynamics in Iron-Starved Mycobacterium tuberculosis Revealed by Turnover and Abundance Measurement Using Hybrid-Linear Ion Trap-Fourier Transform Mass Spectrometry
Rao, P., Rodríguez, G. M., Smith, I., & Li, Q. (2008) · Analytical Chemistry · doi:10.1021/ac800288t · Cited by 33 · see citing works
Self-citation
Phenotypic adaptation of Mycobacterium tuberculosis to host-associated stressors that induce persister formation
Parbhoo, T., Mouton, J., & Sampson, S. L. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.956607 · Cited by 36 · see citing works
Iron homeostasis in Mycobacterium tuberculosis is essential for persistence
Pandey, M., Talwar, S., Bose, S., & Pandey, A. K. (2018) · Scientific Reports · doi:10.1038/s41598-018-35012-3 · Cited by 32 · see citing works
Production of mycobacterial cell wall glycopeptidolipids requires a member of the MbtH-like protein family
Tatham, E., Chavadi, S. S., Mohandas, P., Edupuganti, U. R., Angala, S. K., Chatterjee, D., & Quadri, L. E. N. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-118 · Cited by 31 · see citing works
Chapter 12 Polyketide Versatility in the Biosynthesis of Complex Mycobacterial Cell Wall Lipids
Chopra, T., & Gokhale, R. S. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)04612-6 · Cited by 31 · see citing works
Comparative analyses of transport proteins encoded within the genomes of Mycobacterium tuberculosis and Mycobacterium leprae
Youm, J., & Saier, M. H. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.015 · Cited by 29 · see citing works
The Metal-Dependent Regulators FurA and FurB from Mycobacterium Tuberculosis
Lucarelli, D., Vasil, M. L., Meyer‐Klaucke, W., & Pohl, E. (2008) · International Journal of Molecular Sciences · doi:10.3390/ijms9081548 · Cited by 28 · see citing works
In Vitro and In Vivo Inhibition of the Mycobacterium tuberculosis Phosphopantetheinyl Transferase PptT by Amidinoureas
Ottavi, S., Scarry, S. M., Mosior, J., Ling, Y., Roberts, J., Singh, A., Zhang, D., Goullieux, L., Roubert, C., Bacqué, E., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01565 · Cited by 27 · see citing works
A description of genes of Corynebacterium pseudotuberculosis useful in diagnostics and vaccine applications
D’Afonseca, V., Moraes, P. M., Dorella, F. A., Pacheco, L. G. C., Meyer, R., Portela, R. W., Miyoshi, A., & Azevedo, V. (2008) · Genetics and Molecular Research · doi:10.4238/vol7-1gmr438 · Cited by 27 · see citing works
An assay to compare the infectivity of Mycobacterium tuberculosis isolates based on aerosol infection of guinea pigs and assessment of bacteriology
Williams, A., James, B. W., Bacon, J., Hatch, K. A., Hatch, G. J., Hall, G. A., & Marsh, P. D. (2004) · Tuberculosis · doi:10.1016/j.tube.2004.11.001 · Cited by 27 · see citing works
A new approach to isolating siderophore-producing actinobacteria
Nakouti, I., Sihanonth, P., & Hobbs, G. (2012) · Letters in Applied Microbiology · doi:10.1111/j.1472-765x.2012.03259.x · Cited by 26 · see citing works
Bacterioferritin nanocage: Structure, biological function, catalytic mechanism, self-assembly and potential applications
Guo, M., Gao, M., Liu, J., Xu, N., & Wang, H. (2022) · Biotechnology Advances · doi:10.1016/j.biotechadv.2022.108057 · Cited by 24 · see citing works
Iron homeostasis and progression to pulmonary tuberculosis disease among household contacts
Minchella, P. A., Donkor, S. A., McDermid, J. M., & Sutherland, J. S. (2015) · Tuberculosis · doi:10.1016/j.tube.2015.02.042 · Cited by 23 · see citing works
Mycobacterium tuberculosisProtein Rv3841 Activates Dendritic Cells and Contributes to a T Helper 1 Immune Response
Choi, S., Choi, H., Shin, K., Back, Y. W., Park, H., Lee, J. H., & Kim, H. (2018) · Journal of Immunology Research · doi:10.1155/2018/3525302 · Cited by 20 · see citing works
Altered drug efflux under iron deprivation unveils abrogated MmpL3 driven mycolic acid transport and fluidity in mycobacteria
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Authors: Rodriguez, G. M., & Smith, I.
Affiliations: International Center for Public Health (US)
Corresponding author: Smith, Issar
Venue: Molecular Microbiology
Publisher: Wiley
Published: 2003-03
Volume: 47
Issue: 6
Pages: 1485-1494
ISSN: 0950-382X (ISSN-L)
1365-2958
DOI: 10.1046/j.1365-2958.2003.03384.x
OpenAlex: W2156343505
Cited by: 162
References: 81
Citations by year: 2026: 4 · 2025: 2 · 2024: 2 · 2023: 3 · 2022: 4 · 2021: 1 · 2020: 6 · 2019: 4 · 2018: 8 · 2017: 4 · 2016: 5 · 2015: 5 · 2014: 6 · 2013: 7 · 2012: 5
FWCI: 2.09
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 4 d)
Locations: Molecular Microbiology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Heart, Lung, and Blood Institute (HL64544, R01HL064544)
National Institute of Allergy and Infectious Diseases (AI-44856)
Topics: Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Keywords: iron regulation, mycobacteria, Mycobacterium tuberculosis, IdeR, iron acquisition, iron storage, oxidative stress response, virulence, iron deficiency, transcriptional regulation
MeSH terms: Iron, Mycobacterium, Virulence, Gene Expression Regulation, Bacterial, Oxidative Stress, Feedback, Physiological

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Mechanisms of iron regulation in mycobacteria: role in physiology and virulence

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