proapoptotic influenza A virus protein PB1-F2 regulates viral polymerase activity by interaction with the PB1 protein

The 11th influenza A virus protein PB1-F2 was previously shown to enhance apoptosis in response to cytotoxic stimuli. The 87 amino acid protein that is encoded by an alternative reading frame of the PB1 polymerase gene was described to localize to mitochondria consistent with its proapoptotic functi...

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Bibliographic Details
Published in:Cellular microbiology 2008-05, Vol.10 (5), p.1140-1152
Main Authors: Mazur, Igor, Anhlan, Darisuren, Mitzner, David, Wixler, Ludmilla, Schubert, Ulrich, Ludwig, Stephan
Format: Article
Language:English
Subjects:
Animals
Cell Line
Cytoplasm - chemistry
Cytoplasm - metabolism
Dogs
Humans
Influenza A virus
RNA Replicase - metabolism
Two-Hybrid System Techniques
Viral Proteins - analysis
Viral Proteins - genetics
Viral Proteins - metabolism
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Summary:The 11th influenza A virus protein PB1-F2 was previously shown to enhance apoptosis in response to cytotoxic stimuli. The 87 amino acid protein that is encoded by an alternative reading frame of the PB1 polymerase gene was described to localize to mitochondria consistent with its proapoptotic function. However, PB1-F2 is also found diffusely distributed in the cytoplasm and in the nucleus suggesting additional functions of the protein. Here we show that PB1-F2 colocalizes and directly interacts with the viral PB1 polymerase protein. Lack of PB1-F2 during infection resulted in an altered localization of PB1 and decreased viral polymerase activity. Consequently, mutant viruses devoid of a functional PB1-F2 reading frame exhibited a small plaque phenotype. Thus, we have identified a novel function of PB1-F2 as an indirect regulator of the influenza virus polymerase activity via its interaction with PB1.
ISSN:1462-5814
1462-5822
DOI:10.1111/j.1462-5822.2008.01116.x