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Nutritional immunity: transition metals at the pathogen–host interface
Open accessAbstract
Transition metals occupy an essential niche in biological systems. Their electrostatic properties stabilize substrates or reaction intermediates in the active sites of enzymes, and their heightened reactivity is harnessed for catalysis. However, this heightened activity also renders transition metals toxic at high concentrations. Bacteria, like all living organisms, must regulate their intracellular levels of these elements to satisfy their physiological needs while avoiding harm. It is therefore not surprising that the host capitalizes on both the essentiality and toxicity of transition metals to defend against bacterial invaders. This Review discusses established and emerging paradigms in nutrient metal homeostasis at the pathogen-host interface.
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In the citing paper
“Haptoglobin and haemopexin rapidly bind hemoglobin and haem released from erythrocytes respectively for iron recycling and to possible avoid toxicity posed by free haem (Kumar and Bandyopadhyay, 2005; Hood and Skaar, 2012).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Hood and Skaar, 2012
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Fe is a redox- active trace metal that has important roles in most biological systems, supporting vital processes such as DNA replication, transcription and central metabolism 9 .”
From Nutritional immunity: the battle for nutrient metals at the host–pathogen interface (2022) · cites this paper as [9]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Due to host nutritional immunity and iron (Fe) sequestration, S. aureus experiences Fe limitation during infection.”
From The oxidative stress regulator, PerR, is required for staphyloferrin B-mediated iron acquisition in Staphylococcus aureus (2026) · cites this paper as [7]
The cited source says what the claim attributes to it.
In the citing paper
“Although iron is abundant within the earth crust, in the human host, iron is a highly restricted nutrient (Frey and Reed, 2012; Hood and Skaar, 2012).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Hood and Skaar, 2012
The cited source says what the claim attributes to it.
In the citing paper
“The concerted action of these proteins renders host Fe pools largely inaccessible to bacteria that lack highaffinity Fe uptake pathways or systems 9,12,14 .”
From Nutritional immunity: the battle for nutrient metals at the host–pathogen interface (2022) · cites this paper as [9]
The cited source says what the claim attributes to it.
In the citing paper
“Vertebrates have developed numerous strategies to starve bacteria of nutrient metals via a process termed nutritional immunity 6,9,10 .”
From Nutritional immunity: the battle for nutrient metals at the host–pathogen interface (2022) · cites this paper as [9]
The cited source says what the claim attributes to it.
In the citing paper
“The prominent strategies that bacteria use to acquire Fe include the secretion of siderophores and the uptake of siderophore-Fe, haem-Fe or kinetically labile ferrous Fe (ref. 9 ) .”
From Nutritional immunity: the battle for nutrient metals at the host–pathogen interface (2022) · cites this paper as [9]
In the citing paper
“This is an innate defense mechanism known as ‘nutritional immunity’.101”
From Iron metabolism and iron disorders revisited in the hepcidin era (2020) · cites this paper as [101]
In the citing paper
“Two of these proteins, S100A8 and S100A9, form a heterodimeric complex named calprotectin and are mainly expressed by PMN.”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [233]
In the citing paper
“Bacterial periplasmic superoxide-dismutases (SOD) contain zinc or manganese to elaborate their defense against host-mediated oxidative stress, and bacteria thus have a certain need for these metals (233).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [233]
In the citing paper
“In addition, copper plays important roles as a prostethic group for many enzymes such as cytochromes, proteins involved in oxidative phosphorylation or copper/zinc-superoxide dismutase (233).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [233]
In the citing paper
“In addition, S100 proteins can be induced by IL-17 and IL-22, and S100 proteins exert pro-inflammatory activity and may promote chemotaxis of PMN (233, 244).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [233]
In the citing paper
“Components of the S100 protein family bind Zn+2, Cu+2, and Mn+2, which thereby exert anti-microbial activity (233).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [233]
In the citing paper
“Nutritional immunity, a strategy of the immune system to deprive essential nutrients, such as divalent metals including iron, from invading pathogens”
From Iron in immune cell function and host defense (2021) · cites this paper as [16]
In the citing paper
“Nutritional immunity, a strategy of the immune system to deprive essential nutrients, such as divalent metals including iron, from invading pathogens [16,17], has played a fundamental role in survival of primate populations challenged by microbes.”
From Iron in immune cell function and host defense (2021) · cites this paper as [16]
In the citing paper
“The sequestration of free iron by host proteins simultaneously prevents acquisition by microbes, a protective effect termed nutritional immunity (see Glossary) 5, 6.”
From Buried Treasure: Evolutionary Perspectives on Microbial Iron Piracy (2015) · cites this paper as [5]
In the citing paper
“The sequestration of essential iron has emerged as a crucial innate defense system termed nutritional immunity”
From Buried Treasure: Evolutionary Perspectives on Microbial Iron Piracy (2015) · cites this paper as [5]
In the citing paper
“An important host defense strategy against infection, known as “nutritional immunity,” relies on the sequestration of essential molecules, such as iron, preventing the growth of pathogens (2).”
From Iron- and Hepcidin-Independent Downregulation of the Iron Exporter Ferroportin in Macrophages during Salmonella Infection (2017) · cites this paper as [2]
In the citing paper
“where competition for limited Fe resources emerged as an evolutionary conserved host defense strategy against infection in plants (2) and animals (3–5) as well as a microbial virulence factor (6).”
From Innate Nutritional Immunity (2018) · cites this paper as [4]
In the citing paper
“Presumably, this explains why most pathogens evolved a variety of strategies aimed at diverting Fe from their hosts into their own metabolic pathways, while hosts co-evolved strategies to restrict pathogens from accessing Fe (3–6).”
From Innate Nutritional Immunity (2018) · cites this paper as [4]
In the citing paper
“Nutritional immunity has since been expanded to include the host processes that manipulate local levels of manganese, zinc, and other transition metals in order to metal starve or intoxicate the invading pathogens”
From Heme Synthesis and Acquisition in Bacterial Pathogens (2016) · cites this paper as [16]
In the citing paper
“The limited access of pathogens to metals serves as an antimicrobial strategy and limits bacterial replication.”
From Heme Synthesis and Acquisition in Bacterial Pathogens (2016) · cites this paper as [16]
In the citing paper
“Thirty years later, Eugene Weinberg popularized the term nutritional immunity to describe the phenomenon, which has since been expanded to include host restriction of zinc, manganese, and nonmetal nutrients such as amino acids (65, 140, 149).”
From Transition Metals and Virulence in Bacteria (2016) · cites this paper as [65]
In the citing paper
“Conflict exists between hosts and invading pathogens over the control of the critical micronutrient, iron (reviewed in [8,9]).”
From Rapidly Escalating Hepcidin and Associated Serum Iron Starvation Are Features of the Acute Response to Typhoid Infection in Humans (2015) · cites this paper as [9]
In the citing paper
“iron and other components of nutritional immunity (e.g., zinc) regulate essential metabolic and inflammatory pathways in immune cells that are largely uncharacterized (365, 599).”
From Aspergillus fumigatus and Aspergillosis in 2019 (2019) · cites this paper as [365]
In the citing paper
“Most TFs are zinc-dependent proteins, and almost 50% of all eukaryotic enzymes are zinc-containing proteins (365).”
From Aspergillus fumigatus and Aspergillosis in 2019 (2019) · cites this paper as [365]
In the citing paper
“apart from inhibiting pathogen growth, iron and other components of nutritional immunity (e.g., zinc) regulate essential metabolic and inflammatory pathways in immune cells that are largely uncharacterized (365, 599).”
From Aspergillus fumigatus and Aspergillosis in 2019 (2019) · cites this paper as [365]
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Citations
Cites
Escherichia coli and Salmonella :cellular and molecular biology
Neidhardt, F. C. (1996) · ASM Press eBooks · Cited by 8,197
Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
Flo, T. H., Smith, K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., & Aderem, A. (2004) · Nature · doi:10.1038/nature03104 · Cited by 1,877
Urban, C. F., Ermert, D., Schmid, M., Abed, U. A., Goosmann, C., Nacken, W. K. F., Brinkmann, V., Jungblut, P. R., & Zychlinsky, A. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000639 · Cited by 1,720
Mechanisms for copper acquisition, distribution and regulation
Kim, B., Nevitt, T., & Thiele, D. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.72 · Cited by 1,600
Gut inflammation provides a respiratory electron acceptor for Salmonella
Winter, S., Thiennimitr, P., Winter, M. G., Butler, B. P., Huseby, D. L., Crawford, R. W., Russell, J. M., Bevins, C. L., Adams, L. G., Tsolis, R. M., et al. (2010) · Nature · doi:10.1038/nature09415 · Cited by 1,271
Metal ions in biological catalysis: from enzyme databases to general principles
Andreini, C., Bertini, I., Cavallaro, G., Holliday, G. L., & Thornton, J. M. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0404-5 · Cited by 1,150
The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
Macomber, L., & Imlay, J. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812808106 · Cited by 1,117
Metal Chelation and Inhibition of Bacterial Growth in Tissue Abscesses
Corbin, B. D., Seeley, E. H., Raab, A., Feldmann, J., Miller, M. R., Torres, V. J., Anderson, K. L., Dattilo, B. M., Dunman, P. M., Gerads, R., et al. (2008) · Science · doi:10.1126/science.1152449 · Cited by 857
Self-citationBorkow, G., & Gabbay, J. (2005) · Current Medicinal Chemistry · doi:10.2174/0929867054637617 · Cited by 727
Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection
Gläser, R., Harder, J., Lange, H., Bartels, J., Christophers, E., & Schröder, J.-M. (2005) · Nature Immunology · doi:10.1038/ni1142 · Cited by 651
Zinc through the Three Domains of Life
Andreini, C., Banci, L., Bertini, I., & Rosato, A. (2006) · Journal of Proteome Research · doi:10.1021/pr0603699 · Cited by 648
Nutritional immunity beyond iron: a role for manganese and zinc
Kehl-Fie, T. E., & Skaar, E. P. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.11.008 · Cited by 634
Self-citationIntestinal inflammation allows Salmonella to use ethanolamine to compete with the microbiota
Thiennimitr, P., Winter, S., Winter, M. G., Byndloss, M. X., Tolstikov, V., Huseby, D. L., Sterzenbach, T., Tsolis, R. M., Roth, J. R., & Bäumler, A. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107857108 · Cited by 611
Outten, F. W., Huffman, D. L., Hale, J. A., & O’Halloran, T. V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104122200 · Cited by 544
Lack of a role for iron in the Lyme disease pathogen
Posey, J. E., & Gherardini, F. C. (2000) · Science · doi:10.1126/science.288.5471.1651 · Cited by 538
A Role for the ATP7A Copper-transporting ATPase in Macrophage Bactericidal Activity
White, C., Lee, J., Kambe, T., Fritsche, K., & Petris, M. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.070201 · Cited by 524
Iron availability and infection
Weinberg, E. D. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.07.002 · Cited by 516
A Molecular Mechanism for Bacterial Susceptibility to Zinc
McDevitt, C. A., Ogunniyi, A. D., Valkov, E., Lawrence, M. C., Kobe, B., McEwan, A. G., & Paton, J. C. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002357 · Cited by 484
Kehl-Fie, T. E., Chitayat, S., Hood, M. I., Damo, S., Restrepo, N., Garcia, C., Munro, K. A., Chazin, W. J., & Skaar, E. P. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.07.004 · Cited by 419
Self-citationThe Biochemistry of Methane Oxidation
Hakemian, A. S., & Rosenzweig, A. C. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.061505.175355 · Cited by 416
Iron uptake and metabolism in pseudomonads
Cornélis, P. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2550-2 · Cited by 415
Carbon metabolism of intracellular bacterial pathogens and possible links to virulence
Eisenreich, W., Dandekar, T., Heesemann, J., & Goebel, W. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2351 · Cited by 410
Mycobacterial P1-Type ATPases Mediate Resistance to Zinc Poisoning in Human Macrophages
Botella, H., Peyron, P., Levillain, F., Poincloux, R., Poquet, Y., Brandli, I., Wang, C., Tailleux, L., Tilleul, S., Charrière, G. M., et al. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.08.006 · Cited by 381
Dintilhac, A., Alloing, G., Granadel, C., & Claverys, J. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.5111879.x · Cited by 380
Metalloproteomes: A Bioinformatic Approach
Andreini, C., Bertini, I., & Rosato, A. (2009) · Accounts of Chemical Research · doi:10.1021/ar900015x · Cited by 373
Natural Resistance to Intracellular Infections
Jabado, N., Jankowski, A., Dougaparsad, S., Picard, V., Grinstein, S., & Gros, P. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.9.1237 · Cited by 372
Feo – Transport of Ferrous Iron into Bacteria
Cartron, M. L., Maddocks, S., Gillingham, P., Craven, C. J., & Andrews, S. C. (2006) · BioMetals · doi:10.1007/s10534-006-0003-2 · Cited by 366
Are pathogenic bacteria just looking for food? Metabolism and microbial pathogenesis
Rohmer, L., Hocquet, D., & Miller, S. I. (2011) · Trends in Microbiology · doi:10.1016/j.tim.2011.04.003 · Cited by 364
Hantke, K., Nicholson, G., Rabsch, W., & Winkelmann, G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737682100 · Cited by 359
Intracellular Copper Does Not Catalyze the Formation of Oxidative DNA Damage in Escherichia coli
Macomber, L., Rensing, C., & Imlay, J. A. (2007) · Journal of Bacteriology · doi:10.1128/jb.01357-06 · Cited by 356
Role of copper in reducing hospital environment contamination
Casey, A. L., Adams, D., Karpanen, T. J., Lambert, P. A., Cookson, B., Nightingale, P., Miruszenko, L., Shillam, R., Christian, P., & Elliott, T. S. J. (2009) · Journal of Hospital Infection · doi:10.1016/j.jhin.2009.08.018 · Cited by 355
Methanobactin, a Copper-Acquisition Compound from Methane-Oxidizing Bacteria
Kim, H. J., Graham, D. W., DiSpirito, A. A., Alterman, M. A., Galeva, N. A., Larive, C. K., Asunskis, D. J., & Sherwood, P. M. A. (2004) · Science · doi:10.1126/science.1098322 · Cited by 344
Nutritional Immunity: Host's Attempt to Withhold Iron From Microbial Invaders
Weinberg, E. D. (1975) · JAMA · doi:10.1001/jama.1975.03240130021018 · Cited by 342
CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator
Liu, T., Ramesh, A., Ma, Z., Ward, S. K., Zhang, L., George, G. N., Talaat, A. M., Sacchettini, J. C., & Giedroc, D. P. (2007) · Nature Chemical Biology · doi:10.1038/nchembio844 · Cited by 338
Copper resistance is essential for virulence of Mycobacterium tuberculosis
Wolschendorf, F., Ackart, D., Shrestha, T. B., Hascall-Dove, L., Nolan, S., Lamichhane, G., Wang, Y., Bossmann, S. H., Basaraba, R. J., & Niederweis, M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009261108 · Cited by 332
Liu, J. Z., Jellbauer, S., Poe, A. J., Ton, V., Pesciaroli, M., Kehl-Fie, T. E., Restrepo, N. A., Hosking, M. P., Edwards, R. A., Battistoni, A., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.01.017 · Cited by 328
Self-citationManganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
Anjem, A., Varghese, S., & Imlay, J. A. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06699.x · Cited by 324
Bacterial zinc uptake and regulators
Hantke, K. (2005) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.02.001 · Cited by 319
Staphylococcus aureus IsdB Is a Hemoglobin Receptor Required for Heme Iron Utilization
Torres, V. J., Pishchany, G., Humayun, M., Schneewind, O., & Skaar, E. P. (2006) · Journal of Bacteriology · doi:10.1128/jb.01335-06 · Cited by 302
Self-citationXu, F., & Imlay, J. A. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.07368-11 · Cited by 297
Forbes, J. R., & Gros, P. (2003) · Blood · doi:10.1182/blood-2003-02-0425 · Cited by 288
Copper in Microbial Pathogenesis: Meddling with the Metal
Samanovic, M. I., Ding, C., Thiele, D. J., & Darwin, K. H. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.01.009 · Cited by 278
Iron-withholding strategy in innate immunity
Ong, S. T., Shan Ho, J. Z., Ho, B., & Ding, J. L. (2006) · Immunobiology · doi:10.1016/j.imbio.2006.02.004 · Cited by 269
Recent insights into iron import by bacteria
Braun, V., & Hantke, K. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.01.005 · Cited by 264
Structural basis for iron piracy by pathogenic Neisseria
Noinaj, N., Easley, N. C., Oke, M., Mizuno, N., Gumbart, J., Boura, E., Steere, A. N., Zak, O., Aisen, P., Tajkhorshid, E., et al. (2012) · Nature · doi:10.1038/nature10823 · Cited by 262
Identification and characterization of the transferrin receptor from Neisseria meningitidis
Schryvers, A. B., & Morris, L. J. (1988) · Molecular Microbiology · doi:10.1111/j.1365-2958.1988.tb00029.x · Cited by 258
Ammendola, S., Pasquali, P., Pistoia, C., Petrucci, P., Petrarca, P., Rotilio, G., & Battistoni, A. (2007) · Infection and Immunity · doi:10.1128/iai.00559-07 · Cited by 255
Bianchi, M., Niemiec, M. J., Siler, U., Urban, C. F., & Reichenbach, J. (2011) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2011.01.021 · Cited by 254
NETs formed by human neutrophils inhibit growth of the pathogenic mold Aspergillus fumigatus
McCormick, A., Heesemann, L., Wagener, J., Marcos, V., Hartl, D., Loeffler, J., Heesemann, J., & Ebel, F. (2010) · Microbes and Infection · doi:10.1016/j.micinf.2010.06.009 · Cited by 254
Bearden, S. W., & Perry, R. D. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01360.x · Cited by 254
Rokhbakhsh‐Zamin, F., Sachdev, D., Pour, N. K., Engineer, A. S., Pardesi, K. R., Zinjarde, S., Dhakephalkar, P. K., & Chopade, B. A. (2011) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1012.12006 · Cited by 226
Lawrence, M. C., Pilling, P. A., Epa, V. C., Berry, A. M., Ogunniyi, A. D., & Paton, J. C. (1998) · Structure · doi:10.1016/s0969-2126(98)00153-1 · Cited by 224
Sobota, J. M., & Imlay, J. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100410108 · Cited by 223
Host Proteasomal Degradation Generates Amino Acids Essential for Intracellular Bacterial Growth
Price, C. T. D., Al‐Quadan, T., Šantić, M., Rosenshine, I., & Kwaik, Y. A. (2011) · Science · doi:10.1126/science.1212868 · Cited by 217
Brandel, J., Humbert, N., Elhabiri, M., Schalk, I. J., Mislin, G. L. A., & Albrecht‐Gary, A. (2012) · Dalton Transactions · doi:10.1039/c1dt11804h · Cited by 214
Heme Oxygenase: Evolution, Structure, and Mechanism
Wilks, A. (2002) · Antioxidants and Redox Signaling · doi:10.1089/15230860260220102 · Cited by 213
Lemanceau, P., Bauer, P., Kraemer, S. M., & Briat, J. (2009) · Plant and Soil · doi:10.1007/s11104-009-0039-5 · Cited by 209
Naikare, H. K., Palyada, K., Panciera, R. J., Marlow, D. D., & Stintzi, A. P. (2006) · Infection and Immunity · doi:10.1128/iai.00052-06 · Cited by 204
Nutritional Immunology: A Multi-Dimensional Approach
Ponton, F., Wilson, K. L., Cotter, S. C., Raubenheimer, D., & Simpson, S. J. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002223 · Cited by 200
Schaible, U. E., Collins, H. L., Priem, F., & Kaufmann, S. H. E. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020897 · Cited by 198
Anthrax pathogen evades the mammalian immune system through stealth siderophore production
Abergel, R. J., Wilson, M. K., Arceneaux, J. E. L., Hoette, T. M., Strong, R. K., Byers, B. R., & Raymond, K. N. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607055103 · Cited by 198
CtpV: a putative copper exporter required for full virulence of Mycobacterium tuberculosis
Ward, S. K., Abomoelak, B., Hoye, E. A., Steinberg, H. N., & Talaat, A. M. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07273.x · Cited by 198
Survival of bacteria on metallic copper surfaces in a hospital trial
Mikolay, A., Huggett, S., Tikana, L., Grass, G., Braun, J., & Nies, D. H. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2640-1 · Cited by 192
Anti-Infective Protective Properties of S100 Calgranulins
Hsu, K., Champaiboon, C., Guenther, B. D., Sorenson, B. S., Khammanivong, A., Ross, K. F., Geczy, C. L., & Herzberg, M. C. (2009) · Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry · doi:10.2174/187152309789838975 · Cited by 178
SitABCD Is the Alkaline Mn2+Transporter of Salmonella enterica Serovar Typhimurium
Kehres, D. G., Janakiraman, A., Slauch, J. M., & Maguire, M. E. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.12.3159-3166.2002 · Cited by 177
A novel copper‐responsive regulon in Mycobacterium tuberculosis
Festa, R. A., Jones, M. B., Butler‐Wu, S. M., Sinsimer, D., Gerads, R., Bishai, W. R., Peterson, S. N., & Darwin, K. H. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07431.x · Cited by 167
Copper Homeostasis in Salmonella Is Atypical and Copper-CueP Is a Major Periplasmic Metal Complex
Osman, D., Waldron, K. J., Denton, H., Taylor, C. M., Grant, A. J., Mastroeni, P., Robinson, N. J., & Cavet, J. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145953 · Cited by 164
Characterization of staphyloferrin A biosynthetic and transport mutants in Staphylococcus aureus
Beasley, F. C., Vinés, E. D., Grigg, J. C., Zheng, Q., Liu, S., Lajoie, G. A., Murphy, M. E. P., & Heinrichs, D. E. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06698.x · Cited by 163
Tseng, H., Srikhanta, Y. N., McEwan, A. G., & Jennings, M. P. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02460.x · Cited by 162
Heme acquisition by hemophores
Cescau, S., Cwerman‐Thibault, H., Létoffé, S., Delepelaire, P., Wandersman, C., & Biville, F. (2007) · BioMetals · doi:10.1007/s10534-006-9050-y · Cited by 162
W ITHHOLDING AND E XCHANGING I RON : Interactions Between Erwinia spp. and Their Plant Hosts
Expert, D. (1999) · Annual Review of Phytopathology · doi:10.1146/annurev.phyto.37.1.307 · Cited by 159
A battle for iron: host sequestration and Staphylococcus aureus acquisition
Haley, K. P., & Skaar, E. P. (2012) · Microbes and Infection · doi:10.1016/j.micinf.2011.11.001 · Cited by 157
Self-citationShafeeq, S., Yesilkaya, H., Kloosterman, T. G., Narayanan, G., Wandel, M., Andrew, P. W., Kuipers, O. P., & Morrissey, J. A. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07758.x · Cited by 157
Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity
Cassat, J. E., & Skaar, E. P. (2012) · Seminars in Immunopathology · doi:10.1007/s00281-011-0294-4 · Cited by 155
Self-citationMartin, J. E., & Imlay, J. A. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07593.x · Cited by 150
Campoy, S., Jara, M., Busquets, N., de Rozas, A. M. P., Badiola, I., & Barbé, J. (2002) · Infection and Immunity · doi:10.1128/iai.70.8.4721-4725.2002 · Cited by 148
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Pishchany, G., McCoy, A. L., Torres, V. J., Krause, J. C., Crowe, J. E., Fabry, M. E., & Skaar, E. P. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.11.002 · Cited by 146
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Cheung, J., Beasley, F. C., Liu, S., Lajoie, G. A., & Heinrichs, D. E. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06880.x · Cited by 144
Stork, M., Bos, M. P., Jongerius, I., de Kok, N., Schilders, I., Weynants, V. E., Poolman, J. T., & Tommassen, J. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000969 · Cited by 141
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Reniere, M. L., Ukpabi, G. N., Harry, S. R., Stec, D. F., Krull, R., Wright, D. W., Bachmann, B. O., Murphy, M. E., & Skaar, E. P. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07076.x · Cited by 139
Self-citationBayle, L., Chimalapati, S., Schoehn, G., Brown, J., Vernet, T., & Durmort, C. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07862.x · Cited by 137
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Zhou, T., Ma, Y., Kong, X., & Hider, R. C. (2012) · Dalton Transactions · doi:10.1039/c2dt12159j · Cited by 136
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Rosch, J. W., Gao, G., Ridout, G., Wang, Y., & Tuomanen, E. I. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06638.x · Cited by 134
Hoffman, L. R., Richardson, A. R., Houston, L. S., Kulasekara, H. D., Martens‐Habbena, W., Klausen, M., Burns, J. L., Stahl, D. A., Hassett, D. J., Fang, F. C., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000712 · Cited by 130
Klein, J. S., & Lewinson, O. (2011) · Metallomics · doi:10.1039/c1mt00073j · Cited by 128
Schalk, I. J. (2008) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.11.017 · Cited by 122
Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization and function
Moroz, O. V., Burkitt, W., Wittkowski, H., He, W., Ianoul, A. I., Novitskaya, V., Xie, J., Polyakova, O., Lednev, I. K., Shekhtman, A. G., et al. (2009) · BMC Biochemistry · doi:10.1186/1471-2091-10-11 · Cited by 122
Knapp, C. W., Fowle, D. A., Kulczycki, E., Roberts, J. A., & Graham, D. W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702879104 · Cited by 121
Insect transferrins: Multifunctional proteins
Geiser, D. L., & Winzerling, J. J. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.07.011 · Cited by 121
Interplay between manganese and zinc homeostasis in the human pathogen Streptococcus pneumoniae
Jacobsen, F. E., Kazmierczak, K. M., Lisher, J. P., Winkler, M. E., & Giedroc, D. P. (2010) · Metallomics · doi:10.1039/c0mt00050g · Cited by 118
Davis, L. M., Kakuda, T., & DiRita, V. J. (2008) · Journal of Bacteriology · doi:10.1128/jb.01394-08 · Cited by 118
Achard‐Joris, M., Tree, J. J., Holden, J. A., Simpfendorfer, K. R., Wijburg, O. L. C., Strugnell, R. A., Schembri, M. A., Sweet, M. J., Jennings, M. P., & McEwan, A. G. (2010) · Infection and Immunity · doi:10.1128/iai.01208-09 · Cited by 113
Chapter 12 Role of Iron in Plant–Microbe Interactions
Lemanceau, P., Expert, D., Gaymard, F., Bakker, P. A. H. M., & Briat, J. (2009) · Advances in botanical research · doi:10.1016/s0065-2296(09)51012-9 · Cited by 112
Metallobiology of host–pathogen interactions: an intoxicating new insight
Botella, H., Stadthagen, G., Lugo-Villarino, G., de Chastellier, C., & Neyrolles, O. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.01.005 · Cited by 111
Copper methanobactin: a molecule whose time has come
Balasubramanian, R., & Rosenzweig, A. C. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.01.043 · Cited by 109
Structure of the human S100A12–copper complex: implications for host-parasite defence
Moroz, O. V., Antson, A. A., Grist, S. J., Maitland, N. J., Dodson, G. G., Wilson, K. S., Lukanidin, E. M., & Bronstein, I. B. (2003) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444903004700 · Cited by 108
Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis
Chim, N., Iniguez, A., Nguyen, T. Q., & Goulding, C. W. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.025 · Cited by 102
Ogunniyi, A. D., Mahdi, L. K., Jennings, M. P., McEwan, A. G., McDevitt, C. A., der Hoek, M. B. V., Bagley, C. J., Hoffmann, P., Gould, K. A., & Paton, J. C. (2010) · Journal of Bacteriology · doi:10.1128/jb.00064-10 · Cited by 98
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Segond, D., Dellagi, A., Lanquar, V., Rigault, M., Patrit, O., Thomine, S., & Expert, D. (2008) · The Plant Journal · doi:10.1111/j.1365-313x.2008.03775.x · Cited by 98
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Zarantonelli, M.-L., Szatanik, M., Giorgini, D., Hong, E., Huerre, M., Guillou, F., Alonso, J.-M., & Taha, M.-K. (2007) · Infection and Immunity · doi:10.1128/iai.00781-07 · Cited by 97
Dellagi, A., Segond, D., Rigault, M., Fagard, M., Simon, C., Saindrenan, P., & Expert, D. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.138636 · Cited by 96
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Ghazouani, A. E., Baslé, A., Firbank, S. J., Knapp, C. W., Gray, J., Graham, D. W., & Dennison, C. (2011) · Inorganic Chemistry · doi:10.1021/ic101965j · Cited by 95
Anderson, E. S., Paulley, J. T., Gaines, J. M., Valderas, M. W., Martin, D. W., Menscher, E., Brown, T. D., Burns, C. S., & Roop, R. M. (2009) · Infection and Immunity · doi:10.1128/iai.00444-09 · Cited by 92
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Dashper, S. G., Butler, C. A., Lissel, J. P., Paolini, R. A., Hoffmann, B., Veith, P. D., O'Brien-Simpson, N. M., Snelgrove, S. L., Tsiros, J. T., & Reynolds, E. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503896200 · Cited by 90
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Kenney, G. E., & Rosenzweig, A. C. (2011) · ACS Chemical Biology · doi:10.1021/cb2003913 · Cited by 89
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Balasubramanian, R., Kenney, G. E., & Rosenzweig, A. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.284984 · Cited by 89
Veyrier, F. J., Boneca, I. G., Cellier, M. F., & Taha, M.-K. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002261 · Cited by 85
Pandey, A., & Sonti, R. V. (2010) · Journal of Bacteriology · doi:10.1128/jb.01558-09 · Cited by 82
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Calmettes, C., Alcantara, J., Yu, R., Schryvers, A. B., & Moraes, T. F. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2251 · Cited by 81
Transferrin-iron uptake by gram-negative bacteria
Cornelissen, C. N. (2003) · Frontiers in bioscience · doi:10.2741/1076 · Cited by 80
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Wang, S.-C., Lin, K.-H., Chern, J. P. S., Lu, M.-Y., Jou, S.-T., Lin, D.-T., & Lin, K.-S. (2003) · Clinical Infectious Diseases · doi:10.1086/378062 · Cited by 80
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Nobles, C. L., & Maresso, A. W. (2011) · Metallomics · doi:10.1039/c1mt00047k · Cited by 73
Corbett, D., Wang, J., Schuler, S., Lopez-Castejon, G., Glenn, S., Brough, D., Andrew, P. W., Cavet, J. S., & Roberts, I. S. (2012) · Infection and Immunity · doi:10.1128/iai.05904-11 · Cited by 71
Fabian, M., Solomaha, E., Olson, J. S., & Maresso, A. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040915 · Cited by 70
Kallifidas, D., Pascoe, B., Owen, G. A., Strain-Damerell, C. M., Hong, H., & Paget, M. S. B. (2009) · Journal of Bacteriology · doi:10.1128/jb.01022-09 · Cited by 69
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Hohle, T. H., Franck, W. L., Stacey, G., & O'Brian, M. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110137108 · Cited by 66
Nielubowicz, G. R., Smith, S. N., & Mobley, H. L. T. (2010) · Infection and Immunity · doi:10.1128/iai.01220-09 · Cited by 61
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Puri, S., & O'Brian, M. R. (2006) · Journal of Bacteriology · doi:10.1128/jb.00737-06 · Cited by 59
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Hakemian, A. S., Tinberg, C. E., Kondapalli, K. C., Telser, J., Hoffman, B. M., Stemmler, T. L., & Rosenzweig, A. C. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0558140 · Cited by 59
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Kumar, K. K., Jacques, D. A., Pishchany, G., Caradoc-Davies, T. T., Spirig, T., Malmirchegini, G. R., Langley, D. B., Dickson, C. F., Mackay, J. P., Clubb, R., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.287300 · Cited by 58
Self-citationVibrio vulnificus septicemia in a patient with the hemochromatosis HFE C282Y mutation
Gerhard, G. S., Levin, K. A., Goldstein, J. P., Wojnar, M. M., Chorney, M. J., & Belchis, D. A. (2001) · Archives of Pathology & Laboratory Medicine · doi:10.5858/2001-125-1107-vvsiap · Cited by 58
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Honsa, E. S., & Maresso, A. W. (2011) · BioMetals · doi:10.1007/s10534-011-9413-x · Cited by 57
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Höpfner, M., Nitsche, R., Rohr, A., Harms, D., Schubert, S., & Fölsch, U. R. (2001) · Scandinavian Journal of Gastroenterology · doi:10.1080/003655201750066004 · Cited by 56
The structure of the Escherichia coli hemB gene
Li, J. M., Russell, C. S., & Cosloy, S. D. (1989) · Gene · doi:10.1016/0378-1119(89)90394-6 · Cited by 53
Staphylococcus lugdunensis IsdG Liberates Iron from Host Heme
Haley, K. P., Janson, E. M., Heilbronner, S., Foster, T. J., & Skaar, E. P. (2011) · Journal of Bacteriology · doi:10.1128/jb.00436-11 · Cited by 53
Self-citationHou, Z., Narindrasorasak, S., Bhushan, B., Sarkar, B., & Mitra, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107455200 · Cited by 50
Perry, R. D., Craig, S. K., Abney, J., Bobrov, A. G., Kirillina, O., Mier, I., Truszczynska, H., & Fetherston, J. D. (2012) · Microbiology · doi:10.1099/mic.0.053710-0 · Cited by 50
Champion, O. L., Karlyshev, A. V., Cooper, I. A. M., Ford, D. C., Wren, B. W., Duffield, M. L., Oyston, P. C. F., & Titball, R. W. (2010) · Microbiology · doi:10.1099/mic.0.045807-0 · Cited by 50
Huang, J. H., Oefner, P. J., Adi, V., Ratnam, K. K., Ruoss, S. J., TRAKO, E., & Kao, P. N. (1998) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.157.2.9706012 · Cited by 49
Djoko, K. Y., Franiek, J. A., Edwards, J. L., Falsetta, M. L., Kidd, S. P., Potter, A. J., Chen, N. H., Apicella, M. A., Jennings, M. P., & McEwan, A. G. (2011) · Infection and Immunity · doi:10.1128/iai.06163-11 · Cited by 49
Contribution of the FeoB transporter to Streptococcus suis virulence.
Aranda, J., Cortés, P., Garrido, M. E., Fittipaldi, N., Llagostera, M., Gottschalk, M. G., & Barbé, J. (2009) · PubMed · Cited by 48
The biogenic methanobactin is an effective chelator for copper in a rat model for Wilson disease
Summer, K. H., Lichtmannegger, J., Bandow, N. L., Choi, D. W., DiSpirito, A. A., & Michalke, B. (2011) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2010.12.002 · Cited by 48
Edwards, J. L. (2010) · Infection and Immunity · doi:10.1128/iai.01085-09 · Cited by 48
Hsu, Y.-H., Chen, C.-W., Sun, H. S., Jou, R., Lee, J., & Su, I. (2006) · Journal of the Formosan Medical Association · doi:10.1016/s0929-6646(09)60131-5 · Cited by 46
The role of iron uptake in pathogenicity and symbiosis in Photorhabdus luminescens TT01
Watson, R. J., Millichap, P. J., Joyce, S. A., Reynolds, S. E., & Clarke, D. J. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-177 · Cited by 43
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Tanaka, G., Shojima, J., Matsushita, I., Nagai, H., Kurashima, A., Nakata, K., Toyota, E., Kobayashi, N., Kudo, K., & Keicho, N. (2007) · European Respiratory Journal · doi:10.1183/09031936.00042506 · Cited by 42
Kumar, P., Sannigrahi, S., & Tzeng, Y.-L. (2012) · Infection and Immunity · doi:10.1128/iai.05208-11 · Cited by 39
Rosadini, C. V., Gawronski, J. D., Raimunda, D., Argüello, J. M., & Akerley, B. J. (2011) · Infection and Immunity · doi:10.1128/iai.05135-11 · Cited by 38
Survival Advantage of the Hemochromatosis C282Y Mutation
Weinberg, E. D. (2008) · Perspectives in biology and medicine · doi:10.1353/pbm.2008.0001 · Cited by 37
Lu, Z. H., Dameron, C. T., & Solioz, M. (2003) · BioMetals · doi:10.1023/a:1020709307589 · Cited by 36
Kim, H. W., Chan, Q., Afton, S. E., Caruso, J. A., Lai, B., Weintraub, N. L., & Qin, Z. (2012) · Inflammation · doi:10.1007/s10753-011-9302-z · Cited by 35
Nies, D. H., & Grass, G. (2009) · EcoSal Plus · doi:10.1128/ecosalplus.5.4.4.3 · Cited by 31
Kim, J. S., Kim, M. H., Joe, M. H., Song, S. S., Lee, I. S., & Choi, S. (2002) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2002.tb11166.x · Cited by 29
Saito, Y., Saito, K., Hirano, Y., Ikeya, K., Suzuki, H., Shishikura, K., Manno, S., Takakuwa, Y., Nakagawa, K., Iwasa, A., et al. (2002) · The Journal of Pediatrics · doi:10.1067/mpd.2002.121699 · Cited by 27
Zhang, R., Zhang, J., Guo, G., Mao, X., Tong, W., Zhang, Y., Wang, D., Hu, Y., & Zou, Q. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.10.016 · Cited by 26
Andresen, E., Lange, C. G., Strodthoff, D., Goldmann, T., Fischer, N., Sahly, H., Branscheid, D., & Heine, H. (2011) · BMC Pulmonary Medicine · doi:10.1186/1471-2466-11-10 · Cited by 22
Sato, Y. (2002) · Jornal de Pediatria · Cited by 20
Sharan, R., Chhibber, S., & Reed, R. H. (2010) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph8010021 · Cited by 18
Hyperzincemia and hypercalprotectinemia: unsuccessful treatment with tacrolimus
Isidor, B., Poignant, S., Corradini, N., Fouassier, M., Quartier, P., Roth, J., & Picherot, G. (2008) · Acta Paediatrica · doi:10.1111/j.1651-2227.2008.01092.x · Cited by 17
Zhang, R., Zhang, J., Ding, H., Lu, D., Hu, Y., Wang, D.-C., & Zou, Q. (2011) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309111026194 · Cited by 6
Lee, A., & Li, C. H. (2004) · Clinical Infectious Diseases · doi:10.1086/382683 · Cited by 5
Ratliff-Griffin, M., Wilks, A., & Stojiljković, I. (2014) · ASM Press eBooks · doi:10.1128/9781555816544.ch6 · Cited by 2
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Metadata
- Authors
- Hood, M. I., & Skaar, E. P.
- Affiliations
- Vanderbilt University (US)
- Corresponding author
- Skaar, Eric P.
- ORCID
- Skaar, Eric P.
- Venue
- Nature Reviews Microbiology
- Published
- 2012-07-16
- Volume
- 10
- Issue
- 8
- Pages
- 525-537
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- PMC
- PMC3875331
- OpenAlex
- W1964339096
- Cited by
- 1,535
- References
- 154
- Citations by year
- 2026: 132 · 2025: 97 · 2024: 118 · 2023: 107 · 2022: 152 · 2021: 150 · 2020: 129 · 2019: 147 · 2018: 97 · 2017: 115 · 2016: 97 · 2015: 87 · 2014: 52 · 2013: 40 · 2012: 11
- FWCI
- 7.40
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (AI 069233, AI073843, AI091771, R01AI069233, R56AI091771, R01AI073843)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- nutritional immunity, transition metals, metal homeostasis, host-pathogen arms race, metal sequestration, metal toxicity
- MeSH terms
- Bacteria, Food, Humans, Metals, Transition Elements, Host-Pathogen Interactions
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