Candida albicanserythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently ofd-erythroascorbic acid

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Abstract
Candida albicans D-erythroascorbate peroxidase (EAPX1), which can catalyze the oxidation of D-erythroascorbic acid (EASC) to water, was observed to be inducible in EAPX1-deficient and EAPX1-overexpressing cells via activity staining. EAPX1-deficient cells have remarkably increased intracellular reactive oxygen species and methylglyoxal independent of the intracellular EASC content. The increased methylglyoxal caused EAPX1-deficient cells to activate catalase-permddase and cytochrome c peroxidase, which led to defects in cell growth, viability, mitochondria respiration, filamentation and virulence. These findings indicate that EAPX1 mediates cell differentiation and virulence by regulating intracellular methylglyoxal along with oxidative stresses, regardless of endogenous EASC biosynthesis or alternative oxidase expression. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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