The DOI matches its Crossref record; 152 of the 154 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
Flagged first, then by citations
2 of the 154 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 301–400 of 1,005
Lin, D., & Medeiros, D. M. (2023) · Nutrition Research · doi:10.1016/j.nutres.2023.02.007 · Cited by 62
Rice Xa21 primed genes and pathways that are critical for combating bacterial blight infection
Peng, H., Chen, Z., Fang, Z., Zhou, J., Xia, Z., Gao, L., Chen, L., Li, L., Li, T., Zhai, W., et al. (2015) · Scientific Reports · doi:10.1038/srep12165 · Cited by 60
Sanson, M. A., Makthal, N., Flores, A. R., Olsen, R. J., Musser, J. M., & Kumaraswami, M. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1304 · Cited by 60
Shen, Q., Beucler, M. J., Ray, S. C., & Rappleye, C. A. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007444 · Cited by 61
Nam, N. N., Bui, T. L., Son, S. J., & Joo, S. (2019) · Advanced Functional Materials · doi:10.1002/adfm.201809146 · Cited by 60
D’Attoma, G., Morelli, M., Saldarelli, P., Saponari, M., Giampetruzzi, A., Boscia, D., Savino, V., Fuente, L. D. L., & Cobine, P. A. (2019) · Pathogens · doi:10.3390/pathogens8040272 · Cited by 63
G.I. pros: Antimicrobial defense in the gastrointestinal tract
Chung, L. K., & Raffatellu, M. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.02.001 · Cited by 60
Raimunda, D., Long, J. E., Padilla‐Benavides, T., Sassetti, C. M., & ARGÜELLO, J. M. (2013) · Molecular Microbiology · doi:10.1111/mmi.12454 · Cited by 59
Pseudomonas aeruginosa zinc homeostasis: Key issues for an opportunistic pathogen
Gonzalez, M. R., Ducret, V., Leoni, S., & Perron, K. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.01.018 · Cited by 57
Tarifeño-Saldivia, E., Aguilar, A., Contreras, D., Mercado, L. A., Lange, B. M., Márquez, K., Henríquez, A., Riquelme-Vidal, C., & Boltaña, S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01296 · Cited by 59
Interleukin-6 triggers toxic neuronal iron sequestration in response to pathological α-synuclein
Sterling, J. K., Kam, T.-I., Guttha, S., Park, H., Baumann, B., Mehrabani-Tabari, A. A., Schultz, H., Anderson, B., Alnemri, A., Chou, S.-C., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110358 · Cited by 58
Charron‐Lamoureux, V., Haroune, L., Pomerleau, M., Hall, L., Orban, F., Leroux, J., Rizzi, A., Bourassa, J.-S., Fontaine, N., d’Astous, É. V., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38222-0 · Cited by 59
Feeding Uninvited Guests: mTOR and AMPK Set the Table for Intracellular Pathogens
Brunton, J., Steele, S. P., Ziehr, B., Moorman, N. J., & Kawula, T. H. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003552 · Cited by 58
Fine control of metal concentrations is necessary for cells to discern zinc from cobalt
Osman, D., Foster, A. W., Chen, J., Svedaite, K., Steed, J. W., Lurie-Luke, E., Huggins, T. G., & Robinson, N. J. (2017) · Nature Communications · doi:10.1038/s41467-017-02085-z · Cited by 58
The Interface of Vibrio cholerae and the Gut Microbiome
Cho, J. Y., Liu, R., Macbeth, J. C., & Hsiao, A. (2021) · Gut Microbes · doi:10.1080/19490976.2021.1937015 · Cited by 58
Nakashige, T. G., Stephan, J. R., Cunden, L. S., Brophy, M. B., Wommack, A. J., Keegan, B. C., Shearer, J., & Nolan, E. M. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06845 · Cited by 57
Stocks, C. J., Schembri, M. A., Sweet, M. J., & Kapétanovic, R. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.4ri0917-358r · Cited by 58
The Monothiol Glutaredoxin Grx4 Regulates Iron Homeostasis and Virulence in Cryptococcus neoformans
Attarian, R., Hu, G., Caza, M., Sánchez‐León, E., Croll, D., Do, E., Bach, H., Missall, T. A., Lodge, J. K., Jung, W. H., et al. (2018) · mBio · doi:10.1128/mbio.02377-18 · Cited by 61
Potts, A. H., Guo, Y., Ahmer, B. M. M., & Romeo, T. (2019) · PLoS ONE · doi:10.1371/journal.pone.0211430 · Cited by 55
Symbiont-Mediated Defense against Legionella pneumophila in Amoebae
König, L., Wentrup, C., Schulz, F., Wascher, F., Escola, S., Swanson, M. S., Buchrieser, C., & Horn, M. (2019) · mBio · doi:10.1128/mbio.00333-19 · Cited by 57
Ryan, D. J., Patterson, N. H., Putnam, N. E., Wilde, A. D., Weiss, A., Perry, W., Cassat, J. E., Skaar, E. P., Caprioli, R. M., & Spraggins, J. M. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b05889 · Cited by 58
Self-citationDemeure, C. E., Dussurget, O., Fiol, G. M., Guern, A. L., Savin, C., & Pizarro‐Cerdá, J. (2019) · Microbes and Infection · doi:10.1016/j.micinf.2019.06.007 · Cited by 57
Neyrolles, O., Mintz, E., & Catty, P. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00089 · Cited by 56
Iron uptake mechanisms as key virulence factors in bacterial fish pathogens
Lemos, M. L., & Balado, M. (2020) · Journal of Applied Microbiology · doi:10.1111/jam.14595 · Cited by 56
The Legionella pneumophila Dot/Icm type IV secretion system and its effectors
Lockwood, D. C., Amin, H., Costa, T. R. D., & Schroeder, G. N. (2022) · Microbiology · doi:10.1099/mic.0.001187 · Cited by 63
Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking
Capdevila, D. A., Rondón, J. J., Edmonds, K. A., Rocchio, J. S., Dujovne, M. V., & Giedroc, D. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00264 · Cited by 64
Martin, C. J., Carey, A. F., & Fortune, S. M. (2015) · Seminars in Immunopathology · doi:10.1007/s00281-015-0533-1 · Cited by 60
Prete, S. D., Vullo, D., Luca, V. D., Carginale, V., Fonzo, P. D., Osman, S. M., ALOthman, Z. A., Supuran, C. T., & Capasso, C. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.05.029 · Cited by 56
Do, H., Makthal, N., VanderWal, A. R., Rettel, M., Savitski, M. M., Peschek, N., Papenfort, K., Olsen, R. J., Musser, J. M., & Kumaraswami, M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705972114 · Cited by 56
Allosteric control of metal-responsive transcriptional regulators in bacteria
Baksh, K. A., & Zamble, D. B. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.011444 · Cited by 57
Asempa, T. E., Abdelraouf, K., & Nicolau, D. P. (2019) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkz532 · Cited by 55
Manganese homeostasis at the host-pathogen interface and in the host immune system
Wu, Q., Mu, Q., Xia, Z., Min, J., & Wang, F. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.12.006 · Cited by 59
Giulieri, S. G., Guérillot, R., Duchêne, S., Hachani, A., Daniel, D. S., Seemann, T., Davis, J. S., Tong, S. Y. C., Young, B., Wilson, D. J., et al. (2022) · eLife · doi:10.7554/elife.77195 · Cited by 49
Man, M., Zhu, Y., Liu, L., Luo, L., Han, X., Qiu, L., Li, F., Ren, M., & Xing, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012217 · Cited by 56
Clostridioides difficile ferrosome organelles combat nutritional immunity
Pi, H., Sun, R., McBride, J. R., Kruse, A. R. S., Gibson-Corley, K. N., Krystofiak, E. S., Nicholson, M. R., Spraggins, J. M., Zhou, Q., & Skaar, E. P. (2023) · Nature · doi:10.1038/s41586-023-06719-9 · Cited by 54
Self-citationBobrov, A. G., Kirillina, O. A., Fosso, M. Y., Fetherston, J. D., Miller, M. C., VanCleave, T. T., Burlison, J. A., Arnold, W. K., Lawrenz, M. B., Garneau‐Tsodikova, S., et al. (2017) · Metallomics · doi:10.1039/c7mt00126f · Cited by 54
Nutrition and Bipartite Metabolism of Intracellular Pathogens
Best, A., & Kwaik, Y. A. (2019) · Trends in Microbiology · doi:10.1016/j.tim.2018.12.012 · Cited by 52
Iron in intracellular infection: to provide or to deprive?
Silva-Gomes, S., Vale-Costa, S., Appelberg, R., & Gomes, M. S. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00096 · Cited by 51
Mucormycosis: Pathogenesis and Pathology
Challa, S. (2019) · Current Fungal Infection Reports · doi:10.1007/s12281-019-0337-1 · Cited by 56
Humoral regulation of iron metabolism by extracellular vesicles drives antibacterial response
Kuang, H., Dou, G., Cheng, L., Wang, X., Xu, H., Liu, X., Ding, F., Yang, X., Liu, S., Bao, L., et al. (2023) · Nature Metabolism · doi:10.1038/s42255-022-00723-5 · Cited by 53
Stored red blood cell transfusions: iron, inflammation, immunity, and infection
Spitalnik, S. L. (2014) · Transfusion · doi:10.1111/trf.12848 · Cited by 53
Burcham, L. R., Le Breton, Y., Radin, J. N., Spencer, B. L., Deng, L., Hiron, A., Ransom, M. R., Mendonça, J. D. C., Belew, A. T., El-Sayed, N. M., et al. (2020) · mBio · doi:10.1128/mbio.02302-20 · Cited by 47
Bacterial manganese sensing and homeostasis
Waters, L. S. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.01.003 · Cited by 52
Santos, R. E. R. D. S., Batista, B. B., & Neto, J. F. D. S. (2020) · Applied and Environmental Microbiology · doi:10.1128/aem.01620-20 · Cited by 51
Paterson, J. R., Beecroft, M. S., Mulla, R. S., Osman, D., Reeder, N. L., Caserta, J. A., Young, T. R., Pettigrew, C. A., Davies, G. E., Williams, J. A. G., et al. (2021) · Applied and Environmental Microbiology · doi:10.1128/aem.01641-21 · Cited by 53
López, C., Delmonti, J., Bonomo, R. A., & Vila, A. J. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101665 · Cited by 52
Stephan, J. R., & Nolan, E. M. (2015) · Chemical Science · doi:10.1039/c5sc03287c · Cited by 57
Iron Homeostasis Regulates the Genotoxicity of Escherichia coli That Produces Colibactin
Tronnet, S., Garcie, C., Rehm, N., Dobrindt, U., Oswald, É., & Martín, P. (2016) · Infection and Immunity · doi:10.1128/iai.00659-16 · Cited by 59
Polvi, E. J., Averette, A. F., Lee, S. C., Kim, T., Bahn, Y., Veri, A. O., Robbins, N., Heitman, J., & Cowen, L. E. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006350 · Cited by 53
Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study
Ronnebaum, T. A., & Lamb, A. L. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.01.015 · Cited by 52
Price, S. L., Vadyvaloo, V., DeMarco, J. K., Brady, A., Gray, P. A., Kehl-Fie, T. E., Garneau-Tsodikova, S., Perry, R. D., & Lawrenz, M. B. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2104073118 · Cited by 49
Black, B., Lee, C., Horianopoulos, L. C., Jung, W. H., & Kronstad, J. W. (2021) · PLOS Pathogens · doi:10.1371/journal.ppat.1009661 · Cited by 51
Zhang, F., Li, B., Dong, H., Chen, M., Yao, S., Li, J., Zhang, H., Liu, X., Wang, H., Song, N., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa696 · Cited by 49
“Once in the periplasm, ferric-Ent is immediately captured by FepB and then delivered by the ATP-binding cassette (ABC) transporter, FepDGC, into the cytoplasm where the Fe-Ent can be utilized (8,15,16).”
Adhikary, S., Saha, J., Dutta, P., & Pal, A. (2024) · Geomicrobiology Journal · doi:10.1080/01490451.2024.2340517 · Cited by 51
Groshong, A. M., & Blevins, J. S. (2014) · Advances in applied microbiology · doi:10.1016/b978-0-12-800262-9.00002-0 · Cited by 51
Tullius, M. V., Nava, S., & Horwitz, M. A. (2018) · Infection and Immunity · doi:10.1128/iai.00540-18 · Cited by 51
Valenzuela‐Miranda, D., & Gallardo‐Escárate, C. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02877 · Cited by 51
Soldano, A., Yao, H., Chandler, J. R., & Rivera, M. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.9b00398 · Cited by 51
sRNA-controlled iron sparing response in Staphylococci
Coronel-Tellez, R. H., Pospiech, M., Barrault, M., Liu, W., Bordeau, V., Vasnier, C., Felden, B., Sargueil, B., & Bouloc, P. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac648 · Cited by 43
Lipid and fatty acid metabolism in trypanosomatids
de Aquino, G. P., Gomes, M. A. M., Salinas, R. K., & Laranjeira‐Silva, M. F. (2021) · Microbial Cell · doi:10.15698/mic2021.11.764 · Cited by 50
Lights and Shadows on the Therapeutic Use of Antimicrobial Peptides
Bellotti, D., & Remelli, M. (2022) · Molecules · doi:10.3390/molecules27144584 · Cited by 52
Mycobiota and diet-derived fungal xenosiderophores promote Salmonella gastrointestinal colonization
Santus, W., Rana, A. P., Devlin, J. R., Kiernan, K. A., Jacob, C. C., Tjokrosurjo, J., Underhill, D. M., & Behnsen, J. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01267-w · Cited by 53
Mycobacterium tuberculosis and Copper: A Newly Appreciated Defense against an Old Foe?
Darwin, K. H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.640193 · Cited by 50
O'Brien, V. P., Hannan, T. J., Schaeffer, A. J., & Hultgren, S. J. (2014) · Current Opinion in Infectious Diseases · doi:10.1097/qco.0000000000000130 · Cited by 53
Vinella, D., Fischer, F., Vorontsov, E. A., Gallaud, J., Malosse, C., Michel, V., Cavazza, C., Robbe-Saule, M., Richaud, P., Chamot‐Rooke, J., et al. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005312 · Cited by 50
Vignesh, K. S., Figueroa, J. A. L., Porollo, A., Divanovic, S., Caruso, J. A., & Deepe, G. S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.057 · Cited by 50
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 49
New Insights into the Role of Trace Elements in IBD
Gîlcă-Blanariu, G.-E., Diaconescu, S., Ciocoiu, M., & Ștefănescu, G. (2018) · BioMed Research International · doi:10.1155/2018/1813047 · Cited by 53
Discovery of a Novel Antifungal Agent in the Pathogen Box
Mayer, F. L., & Kronstad, J. W. (2017) · mSphere · doi:10.1128/msphere.00120-17 · Cited by 49
Sclerotinia sclerotiorum utilizes host-derived copper for ROS detoxification and infection
Ding, Y., Mei, J., Chai, Y., Yang, W., Mao, Y., Yan, B., Yu, Y., Disi, J. O., Rana, K., Li, J., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008919 · Cited by 54
Surge of mucormycosis during the COVID-19 pandemic
Dam, P., Cardoso, M. H. E. S., Mandal, S., Franco, O. L., Sağıroğlu, P. Ç., Polat, O. A., Kökoğlu, K., Mondal, R., Mandal, A. K., & Öçsoy, İ. (2023) · Travel Medicine and Infectious Disease · doi:10.1016/j.tmaid.2023.102557 · Cited by 53
Ejje, N., Soe, C. Z., Gu, J., & Codd, R. (2013) · Metallomics · doi:10.1039/c3mt00230f · Cited by 49
Dual Zinc Transporter Systems in Vibrio cholerae Promote Competitive Advantages over Gut Microbiome
Sheng, Y., Fan, F., Jensen, O., Zhong, Z., Kan, B., Wang, H., & Zhu, J. (2015) · Infection and Immunity · doi:10.1128/iai.00447-15 · Cited by 48
Liao, H., Cheng, X., Zhu, D., Wang, M., Jia, R., Chen, S., Chen, X., Biville, F., Liu, M., & Cheng, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127506 · Cited by 48
Mycobacterium tuberculosis in the Face of Host-Imposed Nutrient Limitation
Berney, M., & Berney‐Meyer, L. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.tbtb2-0030-2016 · Cited by 50
Heme proteins in lactic acid bacteria
Baureder, M., & Hederstedt, L. (2013) · Advances in Microbial Physiology · doi:10.1016/b978-0-12-410515-7.00001-9 · Cited by 45
Amich, J., Dümig, M., O'Keeffe, G., Binder, J., Doyle, S., Beilhack, A., & Krappmann, S. (2016) · Infection and Immunity · doi:10.1128/iai.01124-15 · Cited by 48
The race between host and sea lice in the Chilean salmon farming: a genomic approach
Gallardo‐Escárate, C., Arriagada, G., Carrera, C., Gonçalves, A. T., Núñez-Acuña, G., Valenzuela‐Miranda, D., & Valenzuela‐Muñoz, V. (2019) · Reviews in Aquaculture · doi:10.1111/raq.12334 · Cited by 48
Zur: Zinc-Sensing Transcriptional Regulator in a Diverse Set of Bacterial Species
Kandari, D., Joshi, H., & Bhatnagar, R. (2021) · Pathogens · doi:10.3390/pathogens10030344 · Cited by 46
Protective role of zinc in the pathogenesis of respiratory diseases
Luan, R., Ding, D., Xue, Q., Li, H., Wang, Y., & Yang, J. (2022) · European Journal of Clinical Nutrition · doi:10.1038/s41430-022-01191-6 · Cited by 48
Adaptation of Candida Albicans to Commensalism in the Gut
Prieto, D., Correia, I., Plá, J., & Román, E. (2016) · Future Microbiology · doi:10.2217/fmb.16.1 · Cited by 51
Wang, H., Liu, Z., Wang, S., Cui, D., Zhang, X., Liu, Y., & Zhang, Y. (2017) · Metallomics · doi:10.1039/c7mt00007c · Cited by 48
Gorden, P. J., Kleinhenz, M. D., Ydstie, J. A., Brick, T. A., Slinden, L., Peterson, M. P., Straub, D. E., & Burkhardt, D. T. (2018) · Journal of Dairy Science · doi:10.3168/jds.2017-14267 · Cited by 48
Sun, Y., Vornhagen, J., Breen, P. A., Forsyth, V. S., Zhao, L., Mobley, H. L. T., & Bachman, M. A. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008010 · Cited by 48
Osa-miR7695 enhances transcriptional priming in defense responses against the rice blast fungus
Sánchez‐Sanuy, F., Peris-Peris, C., Tomiyama, S., Okada, K., Hsing, Y.-I. C., Segundo, B. S., & Campo, S. (2019) · BMC Plant Biology · doi:10.1186/s12870-019-2156-5 · Cited by 48
Manganese Uptake, Mediated by SloABC and MntH, Is Essential for the Fitness of Streptococcus mutans
Kajfasz, J. K., Katrak, C., Ganguly, T., Vargas, J., Wright, L. L., Peters, Z. T., Spatafora, G. A., Abranches, J., & Lemos, J. A. C. (2020) · mSphere · doi:10.1128/msphere.00764-19 · Cited by 47
Viral strategies predisposing to respiratory bacterial superinfections
Rossi, G. A., Fanous, H., & Colin, A. A. (2020) · Pediatric Pulmonology · doi:10.1002/ppul.24699 · Cited by 54
Natale, C. D., Benedictis, I. D., Benedictis, A. D., & Marasco, D. (2020) · Antibiotics · doi:10.3390/antibiotics9060337 · Cited by 48
Blatzer, M., & Latgé, J.-P. (2017) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.11.015 · Cited by 47
A novel hybrid iron regulation network combines features from pathogenic and nonpathogenic yeasts
Gerwien, F., Safyan, A., Wisgott, S., Hille, F., Kaemmer, P., Linde, J., Brunke, S., Kasper, L., & Hube, B. (2016) · mBio · doi:10.1128/mbio.01782-16 · Cited by 47
Ferric Uptake Regulator and Its Role in the Pathogenesis of Nontypeable Haemophilus influenzae
Harrison, A., Santana, E. A., Szelestey, B. R., Newsom, D. E., White, P., & Mason, K. M. (2013) · Infection and Immunity · doi:10.1128/iai.01227-12 · Cited by 47
Hao, X., Lüthje, F. L., Qin, Y., McDevitt, S. F., Lutay, N., Hobman, J. L., Asiani, K., Soncini, F. C., German, N., Zhang, S., et al. (2015) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-015-6749-0 · Cited by 48
Chang, J. C., Jimenez, J. C., & Federle, M. J. (2015) · Molecular Microbiology · doi:10.1111/mmi.13088 · Cited by 46
Zorzoli, A., Grayczyk, J. P., & Alonzo, F. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005933 · Cited by 49
Neumann, W., Gulati, A., & Nolan, E. M. (2016) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2016.09.012 · Cited by 48
Schatzman, S. S., & Culotta, V. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.8b00026 · Cited by 49
Adaptation to iron deficiency in human pathogenic fungi
Martínez‐Pastor, M. T., & Puig, S. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118797 · Cited by 47
Nutritional Modulation of the Microbiome and Immune Response
Burr, A. B. P., Bhattacharjee, A., & Hand, T. W. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000419 · Cited by 50
Ratitong, B., & Pearlman, E. M. (2021) · Current Opinion in Microbiology · doi:10.1016/j.mib.2021.07.018 · Cited by 50
Nutritional ecology, infection and immune defence — exploring the mechanisms
Cotter, S. C., & Al-Shareefi, E. (2021) · Current Opinion in Insect Science · doi:10.1016/j.cois.2021.12.002 · Cited by 46
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
