The DOI matches its Crossref record; 121 of the 121 references it cites were found in a registry or an index.
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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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
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The distinct morphogenic states of Candida albicans
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Cited by
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Candida albicans pathogenicity mechanisms
Mayer, F. L., Wilson, D., & Hube, B. (2013) · Virulence · doi:10.4161/viru.22913 · Cited by 1,848
Self-citationCandida albicans Als3, a multifunctional adhesin and invasin
Liu, Y., & Filler, S. G. (2011) · Eukaryotic Cell · doi:10.1128/ec.00279-10 · Cited by 354
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans
Caza, M., & Kronstad, J. W. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00080 · Cited by 306
Stress adaptation in a pathogenic fungus
Brown, A. J. P., Budge, S., Kaloriti, D., Tillmann, A., Jacobsen, M. D., Yin, Z., Ene, I. V., Bohovych, I., Sandai, D., Kastora, S., et al. (2014) · Journal of Experimental Biology · doi:10.1242/jeb.088930 · Cited by 299
Köhler, J. R., Hube, B., Puccia, R., Casadevall, A., & Perfect, J. R. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.funk-0014-2016 · Cited by 318
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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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