Journal Article

Effects of Influenza A Nucleoprotein on Polymorphonuclear Neutrophil Function

J. Allen D. Cooper, Roxanna Careelen and Rachel Culbreth

in The Journal of Infectious Diseases

Published on behalf of Infectious Diseases Society of America

Volume 173, issue 2, pages 279-284
Published in print February 1996 | ISSN: 0022-1899
Published online February 1996 | e-ISSN: 1537-6613 | DOI: http://dx.doi.org/10.1093/infdis/173.2.279
Effects of Influenza A Nucleoprotein on Polymorphonuclear Neutrophil Function

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Infection with influenza virus is commonly associated with polymorphonuclear neutrophil (PMNL) dysfunction and consequent secondary bacterial pneumonia. A recently isolated human-derived protein that inhibits PMNL chemotaxis and oxidant production shows a striking homology to the influenza A nucleoprotein. In the present study, the effects of purified influenza A nucleoprotein on PMNL chemotaxis, oxidant production, degranulation, and calcium homeostasis were studied. Results of the study demonstrate that purified nucleoprotein inhibits PMNL chemotaxis as well as superoxide production. In addition, purified nucleoprotein induces a rise in PMNL cytosolic calcium concentration in a manner similar to that demonstrated for crude influenza A lysates. In contrast, no difference in FMLP-stimulated PMNL elastase or β glucuronidase release was noted after exposure to nucleoprotein. These studies suggest that the influenza A nucleoprotein may account for some of the neutrophil defect associated with cellular infection by this virus.

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Subjects: Infectious Diseases ; Immunology ; Public Health and Epidemiology ; Microbiology

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