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Deletion of the copper transporter Ca CCC2 reveals two distinct pathways for iron acquisition in Candida albicans
Author(s) -
Weissman Ziva,
Shemer Revital,
Kornitzer Daniel
Publication year - 2002
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2002.02976.x
Subject(s) - candida albicans , biology , complementation , corpus albicans , yeast , phenotype , microbiology and biotechnology , saccharomyces cerevisiae , ceruloplasmin , biochemistry , gene
Summary Efficient iron acquisition is an essential requirement for growth of pathogenic organisms in the iron‐poor host environment. In Saccharomyces cerevisiae , high‐affinity iron import depends on the multicopper ferroxidase ScFet3. ScFet3 biogenesis in the trans ‐Golgi compartment requires a copper‐transporting P‐type ATPase, ScCcc2. Here, we describe the isolation by functional complementation of a Ccc2 homologue from the pathogenic yeast Candida albicans . CaCcc2 is functionally distinct from a previously described C. albicans copper‐transporting P‐type ATPase, CaCrp1, which appears to be specifically involved in copper detoxification. Regulation of Ca CCC2 and the phenotype of the homozygous Ca CCC2 deletion indicate that it is required for high‐affinity iron import, making it the bona fide CCC2 homologue of C. albicans . Remarkably, in a mouse model of systemic infection, the Ca ccc2 Δ strain displayed robust proliferation and no significant reduction in pathogenicity, suggesting the existence of alternative mechanisms of iron uptake from host tissues. We identify haemin and haemoglobin as potential iron sources that can be used by C. albicans in a CaCcc2‐independent manner.