The NOX/DUOX family of NADPH oxidases are transmembrane
proteins generating reactive oxygen species as their
primary enzymatic products. NADPH oxidase (NOX) 1–5
and Dual oxidase (DUOX) 1 and 2 are members of this family.
These enzymes have several biological functions including
immune defense, hormone biosynthesis, fertilization, cell proliferation
and differentiation, extracellular matrix formation
and vascular regulation. They are found in a variety of tissues
such as the airways, salivary glands, colon, thyroid gland and
lymphoid organs. The discovery of NADPH oxidases has drastically
transformed our view of the biology of reactive oxygen
species and oxidative stress. Roles of several isoforms including
DUOX1 and DUOX2 in host innate immune defense
have been implicated and are still being uncovered. DUOX
enzymes highly expressed in the respiratory and salivary gland
epithelium have been proposed as the major sources of hydrogen
peroxide supporting mucosal oxidative antimicrobial
defenses. In this review, we shortly present data on DUOX
discovery, structure and function, and provide a detailed, upto-
date summary of discoveries regarding antibacterial, antiviral,
antifungal, and antiparasitic functions of DUOX enzymes.
We also present all the literature describing the immune
functions of lactoperoxidase, an enzyme working in
partnership with DUOX to produce antimicrobial substances.
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Reactive oxygen species (ROS) produced by NADPH oxidases
can serve as signaling molecules to regulate a variety of
physiological processes in multi-cellular organisms. In the
nematophagous fungus Arthrobotrys oligospora, we found
that ROS were produced during conidial germination, hyphal
extension, and trap formation in the presence of nematodes.
Generation of an AoNoxA knockout strain demonstrated
the crucial role of NADPH oxidase in the production
of ROS in A. oligospora, with trap formation impaired in
the AoNoxA mutant, even in the presence of the nematode
host. In addition, the expression of virulence factor serine
protease P186 was up-regulated in the wild-type strain, but
not in the mutant strain, in the presence of Caenorhabditis
elegans. These results indicate that ROS derived from AoNoxA
are essential for full virulence of A. oligospora in nematodes.
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