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Candida albicans iron acquisition within the host
Open accessAbstract
As a commensal and opportunistic pathogen, Candida albicans possesses a range of determinants that contribute to survival, persistence and virulence. Among this repertoire of fitness and virulence attributes are iron acquisition factors and pathways, which allow fungal cells to gain this essential mineral in the iron-poor environment of the host. The aim of this review is to present the strategies used by C. albicans to exploit host iron reservoirs and their impact on C. albicans pathogenicity. Because iron in the human host is mostly linked to host proteins, pathogens such as C. albicans must possess mechanisms to gain iron from these proteins. Here, we introduce the most important groups of human proteins, including haemoglobin, transferrin, lactoferrin and ferritin, which contain iron and that are potential iron sources for invading microorganisms. We then summarize and discuss the known and proposed strategies by which C. albicans exploits or may exploit iron from host proteins and compare these with strategies from other pathogenic microorganisms.
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“For example, the expression of the ferritin receptor, Als3, increases in the hyphae-associated program, and inhibition of the hyphal form leads to its diminished expression and reduced capability of ferritin-binding (Almeida et al., 2009).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Almeida et al., 2009
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“Due to the spontaneous generation of toxic free radicals by ferrous iron, a multicopper oxidase enzyme is involved in the reconversion of the produced ferrous iron to a ferric state; a reaction known as ferroxidation (reviewed by Kosman, 2003; Almeida et al., 2009).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Almeida et al., 2009
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“A functional ferric reductase has a ferric reductase domain and a FAD and/or NAD binding domain.”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Almeida et al., 2009
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“These domains were absent in two of the reported reductases while another reductase was lacking a FAD and NAD binding domain (reviewed by Almeida et al., 2009).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Almeida et al., 2009
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“Within the C. albicans genome, there are as much as 17 ferric reductase-related genes but not all these genes are likely to be a ferric reductase.”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Almeida et al., 2009
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Cites
Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00055-x · Cited by 2,702
Candida albicans Secreted Aspartyl Proteinases in Virulence and Pathogenesis
Naglik, J. R., Challacombe, S. J., & Hube, B. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.3.400-428.2003 · Cited by 1,179
Self-citationRegulation of ferritin genes and protein
Torti, F. M., & Torti, S. V. (2002) · Blood · doi:10.1182/blood.v99.10.3505 · Cited by 1,173
Bacterial Iron Sources: From Siderophores to Hemophores
Wandersman, C., & Delepelaire, P. (2004) · Annual Review of Microbiology · doi:10.1146/annurev.micro.58.030603.123811 · Cited by 1,095
Schaible, U. E., & Kaufmann, S. H. E. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1046 · Cited by 945
A Clinical Evaluation of Serum Ferritin as an Index of Iron Stores
Lipschitz, D. A., Cook, J. D., & Finch, C. A. (1974) · New England Journal of Medicine · doi:10.1056/nejm197405302902201 · Cited by 934
Calderone, R. (2012) · ASM Press eBooks · Cited by 912
The distinct morphogenic states of Candida albicans
Sudbery, P., Gow, N., & Berman, J. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.05.008 · Cited by 876
Kakhlon, O., & Cabantchik, Z. I. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01006-7 · Cited by 839
Crichton, R. R., & CHARLOTEAUX‐WAUTERS, M. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb11155.x · Cited by 682
Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells
Phan, Q. T., Myers, C. L., Fu, Y., Sheppard, D. C., Yeaman, M. R., Welch, W. H., Ibrahim, A. S., Edwards, J. E., & Filler, S. G. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050064 · Cited by 641
Stoichiometric and site characteristics of the binding of iron to human transferrin
Aisen, P., Leibman, A., & Zweier, J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62337-9 · Cited by 601
The ALS gene family of Candida albicans.
Hoyer, L. L. (2001) · Trends in Microbiology · doi:10.1016/s0966-842x(01)01984-9 · Cited by 540
Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
Yamauchi, K., Tomita, M., Giehl, T. J., & Ellison, R. T. (1993) · Infection and Immunity · doi:10.1128/iai.61.2.719-728.1993 · Cited by 500
Role of Iron in Bacterial Infection
Bullen, J. J., Rogers, H. J., & Griffiths, E. (1978) · Modern aspects of electrochemistry · doi:10.1007/978-3-642-66956-9_1 · Cited by 494
Regulation of Cell-Surface Genes and Biofilm Formation by the C. albicans Transcription Factor Bcr1p
Nobile, C. J., & Mitchell, A. P. (2005) · Current Biology · doi:10.1016/j.cub.2005.05.047 · Cited by 464
On ferritin heterogeneity. Further evidence for heteropolymers.
Arosio, P., Adelman, T. G., & Drysdale, J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34741-5 · Cited by 457
Distinct Roles for Intra- and Extracellular Siderophores during Aspergillus fumigatus Infection
Schrettl, M., Bignell, E., Kragl, C., Sabiha, Y., Loss, O., Eisendle, M., Wallner, A., Arst, H. N., Haynes, K., & Haas, H. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030128 · Cited by 405
Candida albicans proteinases and host/pathogen interactions
Naglik, J. R., Albrecht, A., Bader, O., & Hube, B. (2004) · Cellular Microbiology · doi:10.1111/j.1462-5822.2004.00439.x · Cited by 402
Self-citationContributions of hyphae and hypha-co-regulated genes to Candida albicans virulence
Kumamoto, C. A., & Vinces, M. D. (2005) · Cellular Microbiology · doi:10.1111/j.1462-5822.2005.00616.x · Cited by 394
Iron–sulfur cluster biogenesis and human disease
Rouault, T. A., & Tong, W. H. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.05.008 · Cited by 391
Zheng, X., Wang, Y.-M., & Wang, Y. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600195 · Cited by 339
A High-Affinity Iron Permease Essential for Candida albicans Virulence
Ramanan, N., & Wang, Y. (2000) · Science · doi:10.1126/science.288.5468.1062 · Cited by 336 · cited 3×
“Ftr2 shares 87% protein identity with Ftr1, but FTR2 is induced when higher levels of iron are available and has no impact on fungal virulence (Ramanan & Wang, 2000).”
BackgroundSundstrom, P. (2002) · Cellular Microbiology · doi:10.1046/j.1462-5822.2002.00206.x · Cited by 336
Haas, H. (2003) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-003-1335-2 · Cited by 334
Molecular mechanisms of iron uptake in fungi
Kosman, D. J. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03368.x · Cited by 331
Almeida, R. S., Brunke, S., Albrecht, A., Thewes, S., Laue, M., Edwards, J. E., Filler, S. G., & Hube, B. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000217 · Cited by 330
Self-citationIdentification and Characterization of TUP1-Regulated Genes in Candida albicans
Braun, B. R., Head, W. S., Wang, M. X., & Johnson, A. D. (2000) · Genetics · doi:10.1093/genetics/156.1.31 · Cited by 306
An eight cysteine-containing CFEM domain unique to a group of fungal membrane proteins
Kulkarni, R. D., Kelkar, H. S., & Dean, R. A. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00025-2 · Cited by 294
Zakikhany, K., Naglik, J. R., Schmidt-Westhausen, A., Holland, G., Schaller, M., & Hube, B. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.01009.x · Cited by 288
Self-citationWard, P. P., Uribe-Luna, S., & Conneely, O. M. (2002) · Biochemistry and Cell Biology · doi:10.1139/o01-214 · Cited by 283
Early Embryonic Lethality of H Ferritin Gene Deletion in Mice
Ferreira, C., Bucchini, D., Martin, M.-E., Levi, S., Arosio, P., Grandchamp, B., & Beaumont, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3021 · Cited by 275
Evidence of H- and L-chains have co-operative roles in the iron-uptake mechanism of human ferritin
Levi, S., Yewdall, S. J., Harrison, P. M., Santambrogio, P., Cozzi, A., Rovida, E., Albertini, A., & Arosio, P. (1992) · Biochemical Journal · doi:10.1042/bj2880591 · Cited by 268
SreA‐mediated iron regulation in Aspergillus fumigatus
Schrettl, M., Kim, H. S., Eisendle, M., Kragl, C., Nierman, W. C., Heinekamp, T., Werner, E. R., Jacobsen, I. D., Illmer, P., Yi, H., et al. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06376.x · Cited by 264
From commensal to pathogen: stage- and tissue-specific gene expression of Candida albicans.
Hube, B. (2004) · Current Opinion in Microbiology · doi:10.1016/j.mib.2004.06.003 · Cited by 260
Self-citationBensen, E. S., Martin, S. J., Li, M., Berman, J. G., & Davis, D. A. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04350.x · Cited by 256
Zhao, X., Oh, S.-H., Cheng, G., Green, C. B., Nuessen, J. A., Yeater, K., Leng, R. P., Brown, A. J. P., & Hoyer, L. L. (2004) · Microbiology · doi:10.1099/mic.0.26943-0 · Cited by 254
Lactoferrin: a multifunctional glycoprotein.
Vorland, L. H. (1999) · APMIS · doi:10.1111/j.1699-0463.1999.tb01499.x · Cited by 252
Regulatory networks affected by iron availability in Candida albicans
Lan, C., Rodarte, G., Murillo, L. A., Jones, T., Davis, R. W., Dungan, J., Newport, G., & Agabian, N. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04214.x · Cited by 249
Candida albicans ALS3 and insights into the nature of the ALS gene family
Hoyer, L. L., Payne, T. L., Bell, M., Myers, A. M., & Scherer, S. (1998) · Current Genetics · doi:10.1007/s002940050359 · Cited by 242
Schweizer, A., Rupp, S., Taylor, B. N., Röllinghoff, M., & Schröppel, K. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02132.x · Cited by 232
Weissman, Z., & Kornitzer, D. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04199.x · Cited by 231
Jung, W. H., Sham, A. P., White, R., & Kronstad, J. W. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040410 · Cited by 227
Heymann, P., Gerads, M., Schaller, M., Dromer, F., Winkelmann, G., & Ernst, J. F. (2002) · Infection and Immunity · doi:10.1128/iai.70.9.5246-5255.2002 · Cited by 226
FLETCHER, J., & Huehns, E. R. (1968) · Nature · doi:10.1038/2181211a0 · Cited by 223
Staphylococcus aureus Redirects Central Metabolism to Increase Iron Availability
Friedman, D. B., Stauff, D. L., Pishchany, G., Whitwell, C. W., Torres, V. J., & Skaar, E. P. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020087 · Cited by 222
Furuyama, K., Kaneko, K., & V., P. D. V. (2007) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.213.1 · Cited by 217
Gobin, J., & Horwitz, M. A. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1527 · Cited by 209
Host-Pathogen Interactions: The Role of Iron1,
Doherty, C. P. (2007) · The Journal of Nutrition · doi:10.1093/jn/137.5.1341 · Cited by 186
Urbanowski, J. L., & Piper, R. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38061 · Cited by 184
Structure-Function Relations of Human Hemoglobins
Marengo-Rowe, A. J. (2006) · Baylor University Medical Center Proceedings · doi:10.1080/08998280.2006.11928171 · Cited by 179 · cited 1×
“It is a compact globular protein of approximately 64 kDa comprised of two pairs of polypeptide chains, termed a and b, which assume the structure of an a2b2 tetramer (reviewed in Marengo-Rowe, 2006).”
BackgroundIron Transport Systems in Neisseria meningitidis
Perkins-Balding, D., Ratliff-Griffin, M., & Stojiljkovic, I. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.1.154-171.2004 · Cited by 172
Genetic and environmental causes of variation in basal levels of blood cells
Evans, D. M., Frazer, I. H., & Martin, N. G. (1999) · Twin Research · doi:10.1375/136905299320565735 · Cited by 169
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
Green, C. B., Cheng, G., Chandra, J., Mukherjee, P. K., Ghannoum, M. A., & Hoyer, L. L. (2004) · Microbiology · doi:10.1099/mic.0.26699-0 · Cited by 159
Genetic and environmental causes of variation in basal levels of blood cells
Evans, D. M., Frazer, I. H., & Martin, N. G. (1999) · Twin Research · doi:10.1375/twin.2.4.250 · Cited by 157
Kontoyiannis, D. P., Chamilos, G., Lewis, R. E., Giralt, S., Cortes, J., Raad, I. I., Manning, J. T., & Han, X. (2007) · Cancer · doi:10.1002/cncr.22909 · Cited by 152
Nobile, C. J., Solis, N., Myers, C. L., Fay, A. J., Deneault, J.-S., Nantel, A., Mitchell, A. P., & Filler, S. G. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01198.x · Cited by 150
Infection-related gene expression in Candida albicans
Brown, A. J. P., Odds, F. C., & Gow, N. A. R. (2007) · Current Opinion in Microbiology · doi:10.1016/j.mib.2007.04.001 · Cited by 148
Reductive iron uptake by Candida albicans: role of copper, iron and the TUP1 regulator
Knight, S. A. B., Lesuisse, E., Stearman, R., Klausner, R. D., & Dancis, A. (2002) · Microbiology · doi:10.1099/00221287-148-1-29 · Cited by 145
Niewerth, M., Kunze, D., Seibold, M., Schaller, M., Körting, H. C., & Hube, B. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.6.1805-1817.2003 · Cited by 145
Self-citationIron Acquisition from Transferrin by Candida albicans Depends on the Reductive Pathway
Knight, S. A. B., Vilaire, G., Lesuisse, E., & Dancis, A. (2005) · Infection and Immunity · doi:10.1128/iai.73.9.5482-5492.2005 · Cited by 145
Crusade for iron: iron uptake in unicellular eukaryotes and its significance for virulence
Šuťák, R., Lesuisse, E., Tachezy, J., & Richardson, D. R. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2008.03.005 · Cited by 145
Thewes, S., Kretschmar, M., Park, H., Schaller, M., Filler, S. G., & Hube, B. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05614.x · Cited by 140
Self-citationHaemin uptake and use as an iron source by Candida albicans: role of CaHMX1-encoded haem oxygenase
Santos, R., Buisson, N., Knight, S., Dancis, A., Camadro, J.-M., & Lesuisse, E. (2003) · Microbiology · doi:10.1099/mic.0.26108-0 · Cited by 139
An endocytic mechanism for haemoglobin‐iron acquisition in Candida albicans
Weissman, Z., Shemer, R., Conibear, E., & Kornitzer, D. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06277.x · Cited by 127
Hydroxamate siderophore production by opportunistic and systemic fungal pathogens
Holzberg, M., & Artis, W. M. (1983) · Infection and Immunity · doi:10.1128/iai.40.3.1134-1139.1983 · Cited by 118
Andrés, M. T., Viejo-Díaz, M., & Fierro, J. F. (2008) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01597-07 · Cited by 114
Hissen, A. H. T., Chow, J. M. T., Pinto, L. J., & Moore, M. M. (2004) · Infection and Immunity · doi:10.1128/iai.72.3.1402-1408.2004 · Cited by 113
Structural and immunological relationships of isoferritins in normal and malignant cells.
Arosio, P., YOKOTA, M., & Drysdale, J. W. (1976) · PubMed · Cited by 109
Eck, R., Hundt, S. M., Härtl, A., Roemer, E., & Künkel, W. (1999) · Microbiology · doi:10.1099/00221287-145-9-2415 · Cited by 109
Characterization of a haemolytic factor from Candida albicans
Watanabe, T., Takano, M., Murakami, M., Tanaka, H., Matsuhisa, A., Nakao, N., Mikami, T., Suzuki, M., & Matsumoto, T. (1999) · Microbiology · doi:10.1099/13500872-145-3-689 · Cited by 109
Baek, Y.-U., Li, M., & Davis, D. A. (2008) · Eukaryotic Cell · doi:10.1128/ec.00108-08 · Cited by 109
Sosinska, G. J., de Groot, P. W. J., de Mattos, M. J. T., Dekker, H. L., de Koster, C. G., Hellingwerf, K. J., & Klis, F. M. (2008) · Microbiology · doi:10.1099/mic.0.2007/012617-0 · Cited by 102
Pendrak, M. L., Chao, M. P., Yan, S. S., & Roberts, D. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311550200 · Cited by 97
Hu, C.-J., Bai, C., Zheng, X.-D., Wang, Y.-M., & Wang, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204545200 · Cited by 97
Studies on the mechanism of iron release from transferrin
Morgan, E. H. (1979) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(79)90144-2 · Cited by 95
Ferroxidase kinetics of horse spleen apoferritin.
Sun, S., & Chasteen, N. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74019-8 · Cited by 91
Weissman, Z., Shemer, R., & Kornitzer, D. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02976.x · Cited by 88
Iron acquisition systems for ferric hydroxamates, haemin and haemoglobin in Listeria monocytogenes
Jin, B. K., Newton, S. M. C., Shao, Y., Jiang, X., Charbit, A., & Klebba, P. E. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.05015.x · Cited by 86
Larson, J. A., Howie, H. L., & So, M. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04169.x · Cited by 85
Ueta, E., Tanida, T., & Osaki, T. (2001) · Journal of Peptide Research · doi:10.1111/j.1399-3011.2001.00821.x · Cited by 83
A role for complement receptor-like molecules in iron acquisition by Candida albicans
Moors, M. A., Stull, T. L., Blank, K. J., Buckley, H. R., & Mosser, D. M. (1992) · The Journal of experimental medicine · doi:10.1084/jem.175.6.1643 · Cited by 80
An, Z., Mei, B., Yuan, W. M., & Leong, S. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1742 · Cited by 79
Hammacott, J. E., Williams, P. H., & Cashmore, A. M. (2000) · Microbiology · doi:10.1099/00221287-146-4-869 · Cited by 69
Ardon, O., Bussey, H., Philpott, C., Ward, D. M., Davis-Kaplan, S., Verroneau, S., Jiang, B., & Kaplan, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108701200 · Cited by 68
Siderophore production by the pathogenic yeast, Candida albicans
Ismail, A., Bedell, G. W., & Lupan, D. M. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)90499-1 · Cited by 63
Iron(III) complexation of Desferrioxamine B encapsulated in apoferritin
Dominguez-Vera, J. M. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2003.12.015 · Cited by 61
Pammi, M., & Rong, L. (2008) · Journal of Medical Microbiology · doi:10.1099/jmm.0.2008/001263-0 · Cited by 59
Sigle, H.-C., Thewes, S., Niewerth, M., Körting, H. C., Schäfer‐Korting, M., & Hube, B. (2005) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dki089 · Cited by 58
Self-citationGenome-wide expression profiling of the response to ciclopirox olamine in Candida albicans
Lee, R. B., Liu, T. T., Barker, K. S., Lee, R. E., & Rogers, P. D. (2005) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dki105 · Cited by 57
Iron uptake by fungi: Contrasted mechanisms with internal or external reduction
Luca, N. G. D., & Wood, P. M. (2000) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(00)43002-x · Cited by 56
Lesuisse, E., Knight, S. A. B., Camadro, J., & Dancis, A. (2002) · Yeast · doi:10.1002/yea.840 · Cited by 56
Sensing the host environment: recognition of hemoglobin by the pathogenic yeast Candida albicans
Pendrak, M. L., Yan, S. S., & Roberts, D. D. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.02.006 · Cited by 55
Fang, H., & Wang, Y. (2002) · Biochemical Journal · doi:10.1042/bj20021005 · Cited by 54
Iron and ferritin in inflammation and cancer.
Torti, S. V., & Torti, F. M. (1994) · PubMed · Cited by 53
Receptor-induced switch in site-site cooperativity during iron release by transferrin
Bali, P. K., & Aisen, P. (1992) · Biochemistry · doi:10.1021/bi00131a011 · Cited by 53 · cited 1×
“The proposed mechanism by which transferrin releases iron to other host cells is via binding to the transferrin receptor coupled with acidification to pH 5.6 (Bali & Aisen, 1992).”
BackgroundInfluentialBurkholderia cenocepacia utilizes ferritin as an iron source
Whitby, P. W., VanWagoner, T. M., Springer, J. M., Morton, D. J., Seale, T. W., & Stull, T. L. (2006) · Journal of Medical Microbiology · doi:10.1099/jmm.0.46199-0 · Cited by 53
Antibacterial Effects of Lactoferricin B
Vorland, L. H. (1999) · Scandinavian Journal of Infectious Diseases · doi:10.1080/003655499750006245 · Cited by 53
Tanida, T., Rao, F., Hamada, T., Ueta, E., & Osaki, T. (2001) · Infection and Immunity · doi:10.1128/iai.69.6.3883-3890.2001 · Cited by 50
Outer membrane peptides ofYersinia pestis mediating siderophore-independent assimilation of iron
Sikkema, D. J., & Brubaker, R. R. (1989) · BioMetals · doi:10.1007/bf01142557 · Cited by 49
Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans
Yamada-Okabe, T., Shimmi, O., Doi, R., Mizumoto, K., Arisawa, M., & Yamada-Okabe, H. (1996) · Microbiology · doi:10.1099/00221287-142-9-2515 · Cited by 46 · cited 3×
“…ferric reductases, which are able to reduce insoluble extracellular ferric (Fe31) ions into soluble ferrous (Fe21) ions, have been described: Cfl1/Fre1 (Yamada-Okabe et al., 1996; Hammacott et al., 2000) and Cfl95/Fre10/Rbt2 (Braun et al., 2000; Knight et al., 2002, 2005; Knight & Dancis, 2006).”
BackgroundIron overload exacerbates experimental meningoencephalitis by Cryptococcus neoformans
Barluzzi, R., Saleppico, S., Nocentini, A., Boelaert, J. R., Neglia, R. G., Bistoni, F., & Blasi, E. (2002) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(02)00324-7 · Cited by 44
Bernier, G., Girijavallabhan, V. M., Murray, A. P., Niyaz, N. M., Ding, P., Miller, M. J., & Malouin, F. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.49.1.241-248.2005 · Cited by 42
Endothelial Cell Injury Caused by Candida albicans Is Dependent on Iron
Fratti, R. A., Belanger, P. H., Ghannoum, M. A., Edwards, J. E., & Filler, S. G. (1998) · Infection and Immunity · doi:10.1128/iai.66.1.191-196.1998 · Cited by 40
Hemoglobin Is Utilized byCandida albicansin the Hyphal Form but Not Yeast Form
Tanaka, W. T. H., Nakao, N., Mikami, T., & Matsumoto, T. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6247 · Cited by 40
Hemoglobin Induces Binding of Several Extracellular Matrix Proteins to Candida albicans
Yan, S. S., Rodrigues, R. G., Cahn-Hidalgo, D., Walsh, T. J., & Roberts, D. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5638 · Cited by 39
Froissard, M., Belgareh‐Touzé, N., Dias, M., Buisson, N., Camadro, J., Haguenauer‐Tsapis, R., & Lesuisse, E. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00627.x · Cited by 38
Knight, S. A. B., & Dancis, A. (2006) · Microbiology · doi:10.1099/mic.0.28843-0 · Cited by 37
Green, C. B., Zhao, X., & Hoyer, L. L. (2005) · Infection and Immunity · doi:10.1128/iai.73.3.1852-1855.2005 · Cited by 36
Modification of ferritin during iron loading
Welch, K. D., Eden, M. E. V., & Aust, S. D. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00676-1 · Cited by 30
Infection-Associated Genes of Candida Albicans
Hube, B. (2006) · Future Microbiology · doi:10.2217/17460913.1.2.209 · Cited by 29
Self-citationExperimental candidiasis in iron overload
Abe, F., Tateyma, M., Shibuya, H., Azumi, N., & Ommura, Y. (1985) · Mycopathologia · doi:10.1007/bf00437134 · Cited by 27
Lahoz, E., Pisacane, A., Iannaccone, M., Palumbo, D., & Capparelli, R. (2008) · Natural Product Research · doi:10.1080/14786410701650253 · Cited by 24
Jollès, J., Mazurier, J., Metz‐Boutigue, M., Spik, G., Montreuil, J., & Jollès, P. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80646-1 · Cited by 23
Liang, Y., Gui, L., Wei, D., Zheng, W. L., Xing, L.-J., & Li, M. (2008) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2008.00468.x · Cited by 21
The location of exon boundaries in the multimeric iron-storage protein ferritin
Harrison, P. M., Ford, G. C., Smith, J. M., & White, J. L. (1991) · BioMetals · doi:10.1007/bf01135385 · Cited by 16
Utilization of ferroproteins byCandida albicans during candidastasis by apotransferrin
Han, Y. (2005) · Archives of Pharmacal Research · doi:10.1007/bf02973884 · Cited by 14
Candida albicans can utilize siderophore during candidastasis caused by apotransferrin
Lee, J.-H., & Han, Y. (2006) · Archives of Pharmacal Research · doi:10.1007/bf02969401 · Cited by 11
Hemochromatosis. Common genes, uncommon illness?
Harrison, H., & Adams, P. C. (2002) · PubMed · Cited by 5
Plasma Transferrin Receptor Helps to Predict Iron Deficiency in the Anemia of Chronic Disease
Fleming, D. J., & Wood, R. J. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1995.tb01544.x · Cited by 2
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Self-citation
Metadata
- Authors
- Almeida, R. S., Wilson, D., & Hube, B.
- Affiliations
- Universidade de São Paulo (BR)
- Leibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) (DE)
- Corresponding author
- Hube, Bernhard
- Venue
- FEMS Yeast Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-11
- Volume
- 9
- Issue
- 7
- Pages
- 1000-1012
- ISSN
- 1567-1356 (ISSN-L)
- 1567-1364
- OpenAlex
- W2160042020
- Semantic Scholar
- 4b748f190f18862bde0e478cf1e0d43e77d953bd
- Cited by
- 199
- References
- 120
- Citations by year
- 2026: 2 · 2025: 13 · 2024: 10 · 2023: 11 · 2022: 11 · 2021: 14 · 2020: 10 · 2019: 10 · 2018: 5 · 2017: 17 · 2016: 9 · 2015: 14 · 2014: 18 · 2013: 21 · 2012: 11
- FWCI
- 1.26
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEMS Yeast Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Infectious Diseases › Fungal Infections and Studies
- Keywords
- Candida albicans, iron acquisition, fungal virulence, hemoglobin, transferrin, lactoferrin, ferritin, host-pathogen interaction, fungal pathogenicity
- MeSH terms
- Candida albicans, Humans, Iron, Models, Biological, Virulence
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