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Dual oxidases (DUOX) are enzymes that contain an NADPH oxidase domain that produces hydrogen peroxide (H 2 O 2 ) and a peroxidase domain that can utilize H 2 O 2  to carry out a variety of reactions. The model organism  Caenorhabditis elegans  produces the DUOX, BLI-3, which has roles in both cuticle development and in protection against infection. In previous work, we demonstrated that while certain peroxidases were protective against the human bacterial pathogen  Enterococcus faecalis , the peroxidase domain of BLI-3 was not, leading to the postulate that the NADPH oxidase domain is the basis for BLI-3’s protective effects. In this work, we show that a strain carrying a mutation in the NADPH oxidase domain of BLI-3,  bli-3(im10) , is more susceptible to  E .  faecalis  and the human fungal pathogen  Candida albicans . Additionally, less H 2 O 2  is produced in response to pathogen using both an established Amplex Red assay and a strain of  C .  albicans , WT-OXYellow, which acts as a biosensor of reactive oxygen species (ROS). Finally, a  C .  elegans  line containing a BLI-3::mCherry transgene was generated. Previous work suggested that BLI-3 is produced in the hypodermis and the intestine. Expression of the transgene was observed in both these tissues, and additionally in the pharynx. The amount and pattern of localization of BLI-3 did not change in response to pathogen exposure.

Localization of the Dual Oxidase BLI-3 and Characterization of Its NADPH Oxidase Domain during Infection of Caenorhabditis elegans