Abstract
Extracellular matrices in diverse biological systems are cross-linked by dityrosine covalent bonds catalyzed by the peroxidase/oxidase system. We show that a peroxidase, secreted by the Anopheles gambiae midgut, and dual oxidase form a dityrosine network that decreases gut permeability to immune elicitors. This network protects the microbiota by preventing activation of epithelial immunity. It also provides a suitable environment for malaria parasites to develop within the midgut lumen without inducing nitric oxide synthase expression. Disruption of this barrier results in strong and effective pathogen-specific immune responses.
Publication types
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Research Support, N.I.H., Intramural
MeSH terms
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Animals
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Anopheles / enzymology*
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Anopheles / immunology*
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Anopheles / microbiology
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Anopheles / parasitology
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Anti-Bacterial Agents / pharmacology
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Bacteria / immunology
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Bacterial Physiological Phenomena
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Blood
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Digestive System / enzymology
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Digestive System / immunology
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Digestive System / microbiology
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Digestive System / parasitology
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Enzyme Induction
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Epithelial Cells / immunology
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Epithelial Cells / microbiology
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Epithelial Cells / parasitology
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Extracellular Matrix / metabolism
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Female
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Gene Expression Regulation
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Insect Proteins / metabolism
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Models, Biological
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NADPH Oxidases / genetics
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NADPH Oxidases / metabolism*
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Nitric Oxide Synthase / biosynthesis
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Permeability
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Peroxidase / genetics
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Peroxidase / metabolism*
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Plasmodium berghei / immunology
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Plasmodium berghei / physiology
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Plasmodium falciparum / immunology
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Plasmodium falciparum / physiology
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RNA Interference
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Tyrosine / analogs & derivatives
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Tyrosine / metabolism
Substances
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Anti-Bacterial Agents
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Insect Proteins
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Tyrosine
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dityrosine
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Peroxidase
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Nitric Oxide Synthase
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NADPH Oxidases