Journal
PLOS ONE
Volume 8, Issue 5, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0063852
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Funding
- Medical Research Council [U117585868]
- Medical Research Council [MC_U117585868] Funding Source: researchfish
- MRC [MC_U117585868] Funding Source: UKRI
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PB1-F2, a protein encoded by a second open reading frame of the influenza virus RNA segment 2, has emerged as a modulator of lung inflammatory responses but the molecular mechanisms underlying this are only poorly understood. Here we show that PB1-F2 inhibits the activation of NF-kappa B dependent signalling pathways in luciferase reporter assays. PB1-F2 proteins from four different viruses interact with IKK beta in yeast two-hybrid assays and by co-immunoprecipitation. PB1-F2 expression did not inhibit IKK beta kinase activity or NF-kappa B translocation into the nucleus, but NF-kappa B binding to DNA was severely impaired in PB1-F2 transfected cells as assessed by Electrophoretic Mobility Shift Assay. Neither the N-terminal 57 amino acid truncated forms nor the C-terminus of PB1-F2 were able to inhibit NF-kB dependent signalling, indicating that the full length protein is necessary for the inhibition.
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