AI Article Synopsis
- The PB1-F2 protein of the influenza A virus enhances apoptosis and is primarily located in the mitochondria, but also appears in the cytoplasm and nucleus, indicating potential additional functions.
- PB1-F2 was found to colocalize and interact directly with the viral PB1 polymerase protein, suggesting a functional relationship between them.
- Mutant viruses lacking functional PB1-F2 exhibited decreased polymerase activity and a smaller plaque phenotype, highlighting PB1-F2's role as an indirect regulator of the influenza virus polymerase activity.
Article Abstract
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.
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| http://dx.doi.org/10.1111/j.1462-5822.2008.01116.x | DOI Listing |
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