Superoxide anion production in influenza protein-activated NADPH oxidase of human polymorphonuclear leukocytes.
There are conflicting reports regarding superoxide anion (O2-) production by human polymorphonuclear leukocytes (PMNL) that have been activated by influenza virus. In the present study, the output of O2- 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 O2-: 4.93 nmol of O2-/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 O2- in human PMNL. Neither the hemagglutinating activity of HA nor the enzymatic activity of NA were necessary for viral protein activation of PMNL.
Arora
D J
DJ
Virology Research Center, Institut Armand Frappier, Université du Québec, Laval, Canada.
Henrichon
M
M
D000818:Animals; D004789:Enzyme Activation; D006801:Humans; D009980:Influenza A virus / Q000276:immunology*; D051379:Mice; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D019255:NADPH Oxidases; D009504:Neutrophils / Q000201:enzymology*; D013481:Superoxides / Q000378:metabolism*; D014763:Viral Matrix Proteins / Q000276:immunology*
C031540:M-protein, influenza virus; D014763:Viral Matrix Proteins; D013481:Superoxides; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases