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Superoxide Anion Production in Influenza Protein-Activated NADPH Oxidase of Human Polymorphonuclear Leukocytes

D.J.S. Arora and M. Henrichon
The Journal of Infectious Diseases
Vol. 169, No. 5 (May, 1994), pp. 1129-1133
Published by: Oxford University Press
Stable URL: http://www.jstor.org/stable/30114019
Page Count: 5
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Superoxide Anion Production in Influenza Protein-Activated NADPH Oxidase of Human Polymorphonuclear Leukocytes
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Abstract

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.

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