SUPEROXIDE ANION PRODUCTION IN INFLUENZA PROTEIN-ACTIVATED NADPH OXIDASE OF HUMAN POLYMORPHONUCLEAR LEUKOCYTES

There are conflicting reports regarding superoxide anion (O-2(-)) production by human polymorphonuclear leukocytes (PMNL) that have been activated by influenza virus. In the present study, the output of O-2(-) was determined by measuring superoxide dismutase-inhibitable cytochrome c reduction. Incubation of PMNL with purified influenza matrix (M) protein, neuraminidase (NA), or hemagglutinin (HA) enhanced the production of O-2(-):4.93 nmol of O-2(-)/4 x 10(5) cells/15 min was produced with M protein, 5.20 with NA, and 6.89 with HA. These values were significantly higher (P < .05) than that for untreated PMNL(1.51). Both nonglycosylated and glycosylated proteins had the potential to generate O-2(-) in human PMNL. Neither the hemagglutinating activity of HA nor the enzymatic activity of NA were necessary for viral protein activation of PMNL.