Abstract
Previous studies have shown that most harvests of IAV depress PMNL end-stage functions (oxidative metabolism, degranulation, and chemotaxis) and are called DV. Some harvests affect none of these functions and are called nonDV. Using both DV and nonDV we studied whether IAV induced alterations in protein phosphorylation or changes in F-actin. Using SDS-PAGE and autoradiography (32P), PMNL were incubated with buffer, DV and nonDV to determine if differences in phosphorylation exist in cells stimulated with phorbal myristate acetate. DV, but not nonDV, decreased phosphorylation of multiple proteins including some with Mol. Wts. corresponding to cytoskeletal regulatory proteins and to the myosin light chain. Conversion of G- to F-actin was measured by staining fixed cells with NBD-phallacidin and monitoring fluorescence by flow cytometry. Increases in F-actin occured in DV treated PMNL compared to control. After fMet-Leu-Phe (fMLP) stimulation of PMNL pre-incubated with DV, nonDV or buffer, there was a decrease in peak to prestimulation F-actin fluorescence ratios in both DV and nonDV compared to buffer. Using fluorescence microscopy we compared the regional distribution of labeled virus and the distribution of F-actin in fMLP stimulated PMNL. In polarized cells there was a disassociation between DV (in the uropod) and F-actin (in the lamellipodium). The finding of abnormal phosphorylation may explain the changes in microfilament organization and end-stage functions noted in IAV infected PMNL.
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Wheeler, J., Cassidy, L., Caldwell, S. et al. INFLUENZA A VIRUS (IAV) MAY INDUCE CYTOSKELETON DYSFUNCTION IN POLYMORPHONUCLEAR LEUKOCYTES (PMNL) BY DEPRESSING PROTEIN PHOSPHORYLATION. Pediatr Res 21 (Suppl 4), 320 (1987). https://doi.org/10.1203/00006450-198704010-00918
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DOI: https://doi.org/10.1203/00006450-198704010-00918