title: Epithelial nitration by a peroxidase/NOX5 system mediates mosquito antiplasmodial immunity.
abstract: Plasmodium ookinetes traverse midgut epithelial cells before they encounter the complement system in the mosquito hemolymph. We identified a heme peroxidase (HPX2) and NADPH oxidase 5 (NOX5) as critical mediators of midgut epithelial nitration and antiplasmodial immunity that enhance nitric oxide toxicity in Anopheles gambiae. We show that the two immune mechanisms that target ookinetes-epithelial nitration and thioester-containing protein 1 (TEP1)-mediated lysis-work sequentially, and we propose that epithelial nitration works as an opsonization-like system that promotes activation of the mosquito complement cascade.
authors.affiliation: Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), Rockville, MD 20892, USA.
authors.forename: Giselle de Almeida
authors.initials: Gde A
authors.lastname: Oliveira
authors.forename: Joshua
authors.initials: J
authors.lastname: Lieberman
authors.forename: Carolina
authors.initials: C
authors.lastname: Barillas-Mury
mesh_terms: D000818:Animals; D000852:Anopheles / Q000235:genetics / Q000276:immunology* / Q000502:physiology; D003165:Complement System Proteins / Q000378:metabolism; D005260:Female; D020868:Gene Silencing; D007413:Intestinal Mucosa / Q000276:immunology; D008288:Malaria / Q000276:immunology; D051379:Mice; D008807:Mice, Inbred BALB C; D019255:NADPH Oxidases / Q000235:genetics / Q000378:metabolism*; D009584:Nitrogen / Q000378:metabolism*; D010544:Peroxidases / Q000235:genetics / Q000378:metabolism*; D010962:Plasmodium berghei / Q000276:immunology* / Q000502:physiology
chemical_list: D003165:Complement System Proteins; D010544:Peroxidases; D019255:NADPH Oxidases; D009584:Nitrogen