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Until recently, NADPH oxidase (NOX) enzymes were thought to be a property of multicellularity, where the reactive oxygen species (ROS) produced by NOX acts in signaling processes or in attacking invading microbes through oxidative damage. We demonstrate here that the unicellular yeast and opportunistic fungal pathogen  Candida albicans  is capable of a ROS burst using a member of the NOX enzyme family, which we identify as Fre8.  C .  albicans  can exist in either a unicellular yeast-like budding form or as filamentous multicellular hyphae or pseudohyphae, and the ROS burst of Fre8 begins as cells transition to the hyphal state. Fre8 is induced during hyphal morphogenesis and specifically produces ROS at the growing tip of the polarized cell. The superoxide dismutase Sod5 is co-induced with Fre8 and our findings are consistent with a model in which extracellular Sod5 acts as partner for Fre8, converting Fre8-derived superoxide to the diffusible H 2 O 2  molecule. Mutants of  fre8 Δ/Δ exhibit a morphogenesis defect  in vitro  and are specifically impaired in development or maintenance of elongated hyphae, a defect that is rescued by exogenous sources of H 2 O 2 . A  fre8 Δ/Δ deficiency in hyphal development was similarly observed  in vivo  during  C .  albicans  invasion of the kidney in a mouse model for disseminated candidiasis. Moreover  C .  albicans fre8 Δ/Δ mutants showed defects in a rat catheter model for biofilms. Together these studies demonstrate that like multicellular organisms,  C .  albicans  expresses NOX to produce ROS and this ROS helps drive fungal morphogenesis in the animal host.

Candida albicans FRE8 encodes a member of the NADPH oxidase family that produces a burst of ROS during fungal morphogenesis