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Updated: Feb 4, 2026
Quantifying the Antifungal Activity of Peptides Against Candida albicans
Published on: January 13, 2023
PHO15 genes of Candida albicans and Candida parapsilosis encode HAD-type phosphatases dephosphorylating
Eliška Krocová1, Sylva Neradová2, Rudolf Kupcik1
1Department of Biological and Biochemical Sciences, Faculty of Chemical Technology, University of Pardubice, 532 10 Pardubice, Czech Republic.
Abstract:
Most of the phosphatases of human fungal pathogens Candida albicans and C. parapsilosis have never been experimentally characterised, although dephosphorylation reactions are central to many biological processes. PHO15 genes of these yeasts have been annotated as the sequences encoding 4-nitrophenyl phosphatase, on the basis of homology to PHO13 gene from the bakers' yeast Saccharomyces cerevisiae. To examine the real function of these potential phosphatases from Candida spp., CaPho15p and CpPho15p were prepared using expression in Escherichia coli and characterised. They share the hallmark motifs of the haloacid dehalogenase superfamily, readily hydrolyse 4-nitrophenyl phosphate at pH 8-8.3 and require divalent cations (Mg2+, Mn2+ or Co2+) as cofactors. CaPho15p and CpPho15p did not dephosphorylate phosphopeptides, but rather hydrolysed molecules related to carbohydrate metabolism. The preferred substrate for the both phosphatases was 2-phosphoglycolate. Among the other molecules tested, CaPho15 showed preference for glyceraldehyde phosphate and ß-glycerol phosphate, while CpPho15 dephosphorylated mainly 1,3-dihydroxyacetone phosphate. This type of substrate specificity indicates that CaPho15 and CpPho15 may be a part of metabolic repair system of C. albicans and C. parapsilosis.
Insights
This study characterizes two phosphatases, CaPho15p and CpPho15p, from Candida fungi. These enzymes prefer 2-phosphoglycolate and are involved in carbohydrate metabolism, suggesting a role in metabolic repair.
Area of Science:
- Biochemistry
- Molecular Biology
- Mycology
Background:
- Phosphatases are crucial enzymes in biological processes, but many in human fungal pathogens like Candida albicans and Candida parapsilosis remain uncharacterized.
- PHO15 genes in these yeasts were predicted to encode 4-nitrophenyl phosphatases based on homology to Saccharomyces cerevisiae.
Purpose of the Study:
- To experimentally characterize the function of CaPho15p and CpPho15p from Candida spp.
- To determine the substrate specificity and cofactor requirements of these potential phosphatases.
Main Methods:
- Recombinant expression of CaPho15p and CpPho15p in Escherichia coli.
- Enzymatic assays to determine substrate hydrolysis, pH optimum, and cofactor dependency.
- Analysis of conserved motifs within the haloacid dehalogenase superfamily.
Main Results:
- CaPho15p and CpPho15p hydrolyze 4-nitrophenyl phosphate optimally at pH 8-8.3, requiring divalent cations (Mg2+, Mn2+, or Co2+).
- These phosphatases do not dephosphorylate phosphopeptides but efficiently hydrolyze carbohydrate metabolism-related molecules, with 2-phosphoglycolate as a preferred substrate.
- CaPho15p showed specificity for glyceraldehyde phosphate and ß-glycerol phosphate, while CpPho15p preferred 1,3-dihydroxyacetone phosphate.
Conclusions:
- CaPho15p and CpPho15p belong to the haloacid dehalogenase superfamily.
- Their substrate specificity suggests a role in the metabolic repair systems of Candida albicans and Candida parapsilosis.
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