Iron acquisition, assimilation and regulation in mycobacteria

Banerjee, Sharmistha; Farhana, Aisha; Ehtesham, Nasreen Z.; Hasnain, Seyed E.

doi:10.1016/j.meegid.2011.02.016

Cited by 57Tuberculosis Research and EpidemiologyIron Metabolism and DisordersBacterial Genetics and Biotechnology

Iron acquisition, assimilation and regulation in mycobacteria

Banerjee, Sharmistha, Farhana, Aisha, Ehtesham, Nasreen Z., Hasnain, Seyed E.·2011·Infection, Genetics and Evolution

DOI 10.1016/j.meegid.2011.02.016

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Abstract

Iron is as crucial to the pathogen as it is to the host. The tuberculosis causing bacillus, Mycobacterium tuberculosis (M.tb), is an exceptionally efficient pathogen that has evolved proficient mechanisms to sequester iron from the host despite its thick mycolate-rich outer covering and a highly impermeable membrane of phagolysosome within which it persists inside an infected host macrophage. Further, both overindulgence and moderation of iron inside a host are a threat to mycobacterial persistence. While for removing iron from the host reservoirs, mycobacteria synthesize molecules that have several times higher affinity for iron than their host counterparts, they also synthesize molecules for efficient storage of excess iron. This is supported by tightly regulated iron dependent global gene expressions. In this review we discuss the various molecules and pathways evolved by mycobacteria for an efficient iron metabolism. We also discuss the less investigated players, like iron responsive proteins and iron responsive elements in mycobacteria, and highlight the lacunae in our current understanding of iron acquisition and utilization in mycobacteria with an ultimate aim to make iron metabolism as a possible anti-mycobacterial target.

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M. tuberculosis has evolved an intricate mechanism of acquiring, assimilating, and storing Fe, which determines the fate of the pathogen inside the host.
“Like several other pathogenic bacteria, it has evolved an intricate mechanism of acquiring, assimilating, and storing Fe, which is a component that determines the fate of the pathogen inside the host [28].”
From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [28]
Mycobacteria produce siderophores, which are high-affinity Fe chelators.
“To acquire Fe, mycobacteria produce siderophores (high-affinity Fe chelators).”
From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [28]
M. tuberculosis requires Fe for essential metabolic pathways.
“Similar to most microorganisms, Mycobacterium tuberculosis, the causative agent of tuberculosis, requires Fe for essential metabolic pathways.”
From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [28]
Fur and IdeR are the two key proteins that regulate expression of other Fe-dependent genes.
“Fur and Fe-dependent repressors and activators or IdeR are the two key proteins that regulate expression of other Fe-dependent genes [28, 63].”
From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [28]

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Rv1698 of Mycobacterium tuberculosis Represents a New Class of Channel-forming Outer Membrane Proteins
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Mechanistic Insights into a Novel Exporter-Importer System of Mycobacterium tuberculosis Unravel Its Role in Trafficking of Iron
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Purified Recombinant Hypothetical Protein Coded by Open Reading Frame Rv1885c of Mycobacterium tuberculosis Exhibits a Monofunctional AroQ Class of Periplasmic Chorismate Mutase Activity
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Mechanism of Tuberculostasis in Mammalian Serum II. Induction of Serum Tuberculostasis in Guinea Pigs
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Comparison of Mycobacterium tuberculosis isocitrate dehydrogenases (ICD-1 and ICD-2) reveals differences in coenzyme affinity, oligomeric state, pH tolerance and phylogenetic affiliation
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Distinctiveness of Mycobacterium tuberculosis Genotypes from Human Immunodeficiency Virus Type 1-Seropositive and -Seronegative Patients in Lima, Peru
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In-Vitro Helix Opening of M. tuberculosis oriC by DnaA Occurs at Precise Location and Is Inhibited by IciA Like Protein
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Disruption of the Gene Homologous to MammalianNramp1inMycobacterium tuberculosisDoes Not Affect Virulence in Mice
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The Metal-Dependent Regulators FurA and FurB from Mycobacterium Tuberculosis
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Macrophage: A Cell With Many Faces and Functions in Tuberculosis
Ahmad, F., Rani, A., Alam, A., Zarin, S., Pandey, S., Singh, H., Hasnain, S. E., & Ehtesham, N. Z. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.747799 · Cited by 200 · see citing works
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The PE/PPE multigene family codes for virulence factors and is a possible source of mycobacterial antigenic variation: Perhaps more?
Akhter, Y., Ehebauer, M. T., Mukhopadhyay, S., & Hasnain, S. E. (2011) · Biochimie · doi:10.1016/j.biochi.2011.09.026 · Cited by 162 · see citing works
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A systematic literature review and critical appraisal of epidemiological studies on outdoor air pollution and tuberculosis outcomes
Popović, I., Magalhães, R. J. S., Ge, E., Marks, G. B., Dong, G., Wei, X., & Knibbs, L. D. (2018) · Environmental Research · doi:10.1016/j.envres.2018.12.011 · Cited by 110 · see citing works
Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin
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Mycobacterium tuberculosis Protein PE6 (Rv0335c), a Novel TLR4 Agonist, Evokes an Inflammatory Response and Modulates the Cell Death Pathways in Macrophages to Enhance Intracellular Survival
Sharma, N., Shariq, M., Quadir, N., Singh, J., Sheikh, J. A., Hasnain, S. E., & Ehtesham, N. Z. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.696491 · Cited by 78 · see citing works
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Host iron redistribution as a risk factor for incident tuberculosis in HIV infection: an 11-year retrospective cohort study
McDermid, J. M., Hennig, B. J., van der Sande, M., Hill, A. V., Whittle, H. C., Jaye, A., & Prentice, A. M. (2013) · BMC Infectious Diseases · doi:10.1186/1471-2334-13-48 · Cited by 75 · see citing works
Particle exposures and infections
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Iron acquisition strategies in mycobacteria
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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
A Dual Role of Heme Oxygenase-1 in Tuberculosis
Yang, S., Ouyang, J., Lu, Y., Harypursat, V., & Chen, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.842858 · Cited by 56 · see citing works
Mycobacterium tuberculosis Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) Functions as a Receptor for Human Lactoferrin
Malhotra, H., Patidar, A., Boradia, V. M., Kumar, R., Nimbalkar, R. D., Kumar, A., Gani, Z., Kaur, R., Garg, P., Raje, M., et al. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00245 · Cited by 56 · see citing works
Insights on How the Mycobacterium Tuberculosis Heme Uptake Pathway can Be Used as a Drug Target
Owens, C. P., Chim, N., & Goulding, C. W. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.109 · Cited by 50 · see citing works
Serum proteomics of active tuberculosis patients and contacts reveals unique processes activated during Mycobacterium tuberculosis infection
Mateos, J., Estévez, O., González‐Fernández, Á., Anibarro, L., Pallarés, Á., Reljić, R., Mussá, T., Gomes-Maueia, C., Nguilichane, A., Gallardo, J. M., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-60753-5 · Cited by 52 · 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
“Fur and Fe-dependent repressors and activators or IdeR are the two key proteins that regulate expression of other Fedependent genes [28, 63].”
BackgroundInfluential
Genome-wide Phenotypic Profiling Identifies and Categorizes Genes Required for Mycobacterial Low Iron Fitness
Dragset, M. S., Ioerger, T. R., Zhang, Y. J., Mærk, M., Ginbot, Z., Sacchettini, J. C., Flo, T. H., Rubin, E. J., & Steigedal, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-47905-y · Cited by 49 · see citing works
Iron homeostasis during anemia of inflammation: a prospective study of patients with tuberculosis
Cercamondi, C. I., Stoffel, N. U., Moretti, D., Zöller, T., Swinkels, D. W., Zeder, C., Mhimibra, F., Hella, J., Fenner, L., & Zimmermann, M. B. (2021) · Blood · doi:10.1182/blood.2020010562 · Cited by 43 · 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
Effect of ambient air pollution on tuberculosis risks and mortality in Shandong, China: a multi-city modeling study of the short- and long-term effects of pollutants
Liu, Y., Zhao, S., Li, Y., Song, W.-M., Yu, C., Gao, L., Ran, J., He, D., & Li, H. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-12621-6 · Cited by 38 · see citing works
Regulation of Mycolactone, the Mycobacterium ulcerans Toxin, Depends on Nutrient Source
Deshayes, C., Angala, S. K., Marion, E., Brandli, I., Babonneau, J., Preisser, L., Eyangoh, S. I., Delneste, Y., Legras, P., de Chastellier, C., et al. (2013) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0002502 · Cited by 35 · see citing works
The drug binding sites and transport mechanism of the RND pumps from Mycobacterium tuberculosis: Insights from molecular dynamics simulations
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Impact of fine particulate matter on latent tuberculosis infection and active tuberculosis in older adults: a population-based multicentre cohort study
Guo, T., Tian, S., Xin, H., Du, J., Cao, X., Feng, B., He, Y., He, Y., Wang, D., Zhang, B., et al. (2024) · Emerging Microbes & Infections · doi:10.1080/22221751.2024.2302852 · Cited by 26 · see citing works
Updating and curating metabolic pathways of TB
Slayden, R. A., Jackson, M., Zucker, J., Ramirez, M. V., Dawson, C. C., Crew, R. M., Sampson, N. S., Thomas, S. T., Jamshidi, N., Sisk, P., et al. (2013) · Tuberculosis · doi:10.1016/j.tube.2012.11.001 · Cited by 24 · see citing works
Siderophore transport by MmpL5-MmpS5 protein complex in Mycobacterium tuberculosis
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Cross-Talk Between Iron and Glucose Metabolism in the Establishment of Disease Tolerance
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Quantum dots nanoparticle-based lateral flow assay for rapid detection of Mycobacterium species using anti-FprA antibodies
Cimaglia, F., Aliverti, A., Chiesa, M., Poltronieri, P., Lorenzis, E. D., Santino, A., & Sechi, L. A. (2012) · Nanotechnology Development · doi:10.4081/nd.2012.e5 · Cited by 25 · 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
Stealth Strategies of Mycobacterium tuberculosis for Immune Evasion
Naeem, M. A., Ahmad, W., Tyagi, R., Akram, Q., Younus, M., & Liu, X. (2020) · Current Issues in Molecular Biology · doi:10.21775/cimb.041.597 · Cited by 22 · see citing works
Survival in Hostile Conditions: Pupylation and the Proteasome in Actinobacterial Stress Response Pathways
von Rosen, T., Keller, L. M. L., & Weber-Ban, E. U. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.685757 · Cited by 19 · see citing works
Mass Spectrometry Offers Insight into the Role of Ser/Thr/Tyr Phosphorylation in the Mycobacteria
Calder, B., Albeldas, C., Blackburn, J. M., & Soares, N. C. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00141 · Cited by 19 · see citing works
A Comprehensive Review on the Roles of Metals Mediating Insect–Microbial Pathogen Interactions
Khan, S., & Lang, M. (2023) · Metabolites · doi:10.3390/metabo13070839 · Cited by 21 · see citing works
Targeting Mycobacterium tuberculosis iron-scavenging tools: a recent update on siderophores inhibitors
Kumar, G., & Adhikrao, P. A. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00201b · Cited by 16 · see citing works
Stealing Survival: Iron Acquisition Strategies of Mycobacterium tuberculosis.
Shankar, G., & Akhter, Y. (2024) · Biochimie · doi:10.1016/j.biochi.2024.06.006 · Cited by 12 · see citing works
Tuning the Anti(myco)bacterial Activity of 3-Hydroxy-4-pyridinone Chelators through Fluorophores
Rangel, M., Moniz, T., Silva, A. M. N., & Leite, A. (2018) · Pharmaceuticals · doi:10.3390/ph11040110 · Cited by 15 · see citing works
Transferrin conjugates of antitubercular drug isoniazid: Synthesis and in vitro efficacy
Sutar, Y. B., Mali, J. K., Telvekar, V. N., Rajmani, R. S., & Singh, A. K. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111713 · Cited by 14 · see citing works
Mycobacterium tuberculosis Adaptation to Survival in a Human Host
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ESAT-6 Protein of Mycobacterium tuberculosis Increases Holotransferrin-Mediated Iron Uptake in Macrophages by Downregulating Surface Hemochromatosis Protein HFE
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Authors: Banerjee, S., Farhana, A., Ehtesham, N. Z., & Hasnain, S. E.
Affiliations: University of Hyderabad (IN)
University of Alabama (US)
Jawaharlal Nehru Centre for Advanced Scientific Research (IN)
Corresponding author: Hasnain, Seyed E.
ORCID: Banerjee, Sharmistha
Farhana, Aisha
Ehtesham, Nasreen Z.
Hasnain, Seyed E.
Venue: Infection, Genetics and Evolution
Publisher: Elsevier BV
Published: 2011-07
Volume: 11
Issue: 5
Pages: 825-838
ISSN: 1567-1348 (ISSN-L)
DOI: 10.1016/j.meegid.2011.02.016
OpenAlex: W2095015980
Cited by: 57
References: 132
Citations by year: 2026: 1 · 2025: 1 · 2024: 6 · 2023: 3 · 2022: 6 · 2021: 5 · 2020: 4 · 2019: 2 · 2018: 3 · 2017: 4 · 2016: 4 · 2015: 4 · 2014: 3 · 2013: 8 · 2012: 1
FWCI: 0.56
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Infection Genetics and Evolution (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: iron acquisition, iron metabolism, Mycobacterium tuberculosis, mycobacteria, iron sequestration, iron storage, iron-responsive element, global gene regulation, phagolysosomes, mycolic acids, tuberculosis
MeSH terms: Biological Transport, Humans, Iron, Mycobacterium, Mycobacterium Infections, Gene Expression Regulation, Bacterial

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Iron acquisition, assimilation and regulation in mycobacteria

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