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

Ransome van der Hoeven; Melissa R Cruz; Violeta Chávez; Danielle A Garsin

doi:10.1371/journal.pone.0124091

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

Journal article

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

Ransome van der Hoeven, Melissa R Cruz, Violeta Chávez and Danielle A Garsin

PloS one, Vol.10(4), pp.e0124091-e0124091

04/24/2015

DOI: 10.1371/journal.pone.0124091

PMCID: PMC4409361

PMID: 25909649

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Abstract

Dual oxidases (DUOX) are enzymes that contain an NADPH oxidase domain that produces hydrogen peroxide (H2O2) and a peroxidase domain that can utilize H2O2 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 H2O2 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.

Animals

Animals, Genetically Modified

Caenorhabditis elegans - metabolism

Caenorhabditis elegans - microbiology

Caenorhabditis elegans Proteins - chemistry

Caenorhabditis elegans Proteins - genetics

Caenorhabditis elegans Proteins - metabolism

Disease Susceptibility

Hydrogen Peroxide - metabolism

Mutation

NADPH Oxidases - metabolism

Oxidoreductases - chemistry

Oxidoreductases - genetics

Oxidoreductases - metabolism

Protein Interaction Domains and Motifs

Protein Transport

Details

Title: Subtitle: Localization of the Dual Oxidase BLI-3 and Characterization of Its NADPH Oxidase Domain during Infection of Caenorhabditis elegans
Creators: Ransome van der Hoeven - The University of Texas Health Science Center at Houston
Melissa R Cruz - The University of Texas Health Science Center at Houston
Violeta Chávez - The University of Texas Health Science Center at Houston
Danielle A Garsin - The University of Texas Health Science Center at Houston
Resource Type: Journal article
Publication Details: PloS one, Vol.10(4), pp.e0124091-e0124091
DOI: 10.1371/journal.pone.0124091
PMID: 25909649
PMCID: PMC4409361
NLM abbreviation: PLoS One
ISSN: 1932-6203
eISSN: 1932-6203
Grant note: R01 AI076406 / NIAID NIH HHS R01 AI110432 / NIAID NIH HHS R01AI076406 / NIAID NIH HHS
Language: English
Date published: 04/24/2015
Academic Unit: Dental Research; Periodontics
Record Identifier: 9984737968402771

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