ArticleAntimicrobial agents and chemotherapy2003
Functional similarities and differences between Candida albicans Cdr1p and Cdr2p transporters.
Article in Antimicrobial agents and chemotherapy, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 58 citations in OpenAlex.
- Generation of antifungals to combat drug resistance using language models and diffusion models.Journal of advanced research · 2026Article
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- A putative ABC transporter gene,Microbiology spectrum · 2025Article
- Understanding the mechanisms of resistance to azole antifungals inJAC-antimicrobial resistance · 2025Review
- Functional analysis of Candida albicans Cdr1 through homologous and heterologous expression studies.FEMS yeast research · 2025Review
- Analysis of the Properties of 44 ABC Transporter Genes from Biocontrol AgentCurrent issues in molecular biology · 2023Article
- Characterization of Three Pleiotropic Drug Resistance Transporter Genes and Their Participation in the Azole Resistance ofFrontiers in cellular and infection microbiology · 2021Article
- Phospholipid biosynthesis disruption renders the yeast cells sensitive to antifungals.Folia microbiologica · 2020Article
- Synthetic Organotellurium Compounds Sensitize Drug-Resistant Candida albicans Clinical Isolates to Fluconazole.Antimicrobial agents and chemotherapy · 2017Article
- Beauvericin Potentiates Azole Activity via Inhibition of Multidrug Efflux, Blocks Candida albicans Morphogenesis, and Is Effluxed via Yor1 and Circuitry Controlled by Zcf29.Antimicrobial agents and chemotherapy · 2016Article
- Positive regulation of the Candida albicans multidrug efflux pump Cdr1p function by phosphorylation of its N-terminal extension.The Journal of antimicrobial chemotherapy · 2016Article
- Article
- Rationally designed transmembrane peptide mimics of the multidrug transporter protein Cdr1 act as antagonists to selectively block drug efflux and chemosensitize azole-resistant clinical isolates of Candida albicans.The Journal of biological chemistry · 2013Article
- Candida infections and their prevention.ISRN preventive medicine · 2013Review
- Functionally Relevant Residues of Cdr1p: A Multidrug ABC Transporter of Human Pathogenic Candida albicans.Journal of amino acids · 2011Article
- Farnesol-induced apoptosis in Candida albicans is mediated by Cdr1-p extrusion and depletion of intracellular glutathione.PloS one · 2011Article
- Fluconazole transport into Candida albicans secretory vesicles by the membrane proteins Cdr1p, Cdr2p, and Mdr1p.Eukaryotic cell · 2010Article
- Fungal PDR transporters: Phylogeny, topology, motifs and function.Fungal genetics and biology : FG & B · 2010Review
- Identification of Nile red as a fluorescent substrate of the Candida albicans ATP-binding cassette transporters Cdr1p and Cdr2p and the major facilitator superfamily transporter Mdr1p.Analytical biochemistry · 2009Article
- Oligomerization of human ATP-binding cassette transporters and its potential significance in human disease.Expert opinion on drug metabolism & toxicology · 2009Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Candida albicans CDR1 and CDR2 genes code for highly homologous ATP-binding cassette (ABC) transporters which are overexpressed in azole-resistant clinical isolates and which confer resistance to multiple drugs by actively transporting their substrates out of the cells. These transporters are formed by two homologous halves, each with an intracellular domain containing an ATP-binding site followed by a membrane-associated domain. We have expressed Cdr1p and Cdr2p in Saccharomyces cerevisiae to investigate their functions. The two proteins were properly expressed and functional, as determined by Western blotting, drug susceptibility assays, and rhodamine efflux. Using total membrane proteins from these transformants, we showed that Cdr1p and Cdr2p bind to the photoreactive analogue of rhodamine 123, [(125)I]iodoaryl azido-rhodamine 123 (IAARh123). IAARh123 photoaffinity labeling of membranes prepared from cells expressing either the N half or the C half of Cdr2p, or both, demonstrated that both halves contribute to rhodamine binding and can bind to rhodamine independently. Interestingly, Cdr1p was found to confer hypersusceptibility to FK520, an immunosuppressant and antifungal agent, whereas Cdr2p conferred resistance to this compound, uncovering a major functional difference between the two transporters. Furthermore, when administered in combination with azoles, FK520 sensitized cells expressing CDR1 but not those expressing CDR2. Finally, we showed that Cdr2p confers hypersusceptibility to hydrogen peroxide and resistance to diamide, while Cdr1p has no effect against these oxidative agents. Taken together, our results demonstrate that, despite a high level of structural conservation, Cdr1p and Cdr2p exhibit major functional differences, suggesting distinct biological functions.
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