title: Mechanisms of destruction of Aspergillus fumigatus hyphae mediated by human monocytes.
abstract: Normal monocytes attached to and destroyed Aspergillus hyphae by morphologic and metabolic criteria. Inhibition by anaerobiosis, azide, cyanide, halide-free conditions, catalase, histidine, and tryptophan suggested mediation of hyphal damage primarily through the myeloperoxidase system. However, myeloperoxidase-independent oxidative or nonoxidative mechanisms appeared active in hyphal damage by monocytes from patients with myeloperoxidase deficiency or chronic granulomatous disease (CGD). Moreover, hyphae were damaged by lysates and granule-enriched fractions of monocytes from patients with CGD, whereas comparable fractions of normal monocytes were active only with added halide and H2O2. Hyphal damage by both whole monocytes and granule-enriched fractions from patients with CGD was inhibited by polyanions, a result suggesting that cationic proteins may be involved. Hyphal damage by normal monocytes or monocytes from patients with CGD was inhibited by cells that lacked antihyphal activity (chlorpromazine-treated normal neutrophils or neutrophils from patients with CGD, respectively). This effect may predispose patients with CGD to chronic, invasive aspergillosis.
mesh_terms: D001228:Aspergillosis / Q000276:immunology*; D001232:Aspergillus fumigatus / Q000648:ultrastructure; D003602:Cytotoxicity, Immunologic; D005260:Female; D006105:Granulomatous Disease, Chronic / Q000276:immunology; D006801:Humans; D008297:Male; D009000:Monocytes / Q000502:physiology* / Q000648:ultrastructure; D009504:Neutrophils / Q000502:physiology; D009195:Peroxidase / Q000172:deficiency / Q000502:physiology
chemical_list: D009195:Peroxidase