1. New Interactors of the Truncated EBNA-LP Protein Identified by Mass Spectrometry in P3HR1 Burkitt's Lymphoma Cells.
- Author
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Chelouah, Sonia, Cochet, Emilie, Couvé, Sophie, Balkaran, Sandy, Robert, Aude, May, Evelyne, Ogryzko, Vasily, and Wiels, Joëlle
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PROTEIN metabolism , *APOPTOSIS , *B cell lymphoma , *CELL lines , *ESTERASES , *GENE expression , *MASS spectrometry , *TRANSCRIPTION factors , *VIRAL antigens , *WESTERN immunoblotting , *PRECIPITIN tests - Abstract
The Epstein-Barr virus nuclear antigen leader protein (EBNA-LP) acts as a co-activator of EBNA-2, a transcriptional activator essential for Epstein-Barr virus (EBV)-induced B-cell transformation. Burkitt's lymphoma (BL) cells harboring a mutant EBV strain that lacks both the EBNA-2 gene and 30 exons of EBNA-LP express Y1Y2-truncated isoforms of EBNA-LP (tEBNA-LP) and better resist apoptosis than if infected with the wild-type virus. In such BL cells, tEBNA-LP interacts with the protein phosphatase 2A (PP2A) catalytic subunit (PP2A C), and this interaction likely plays a role in resistance to apoptosis. Here, 28 cellular and four viral proteins have been identified by mass spectrometry as further possible interactors of tEBNA-LP. Three interactions were confirmed by immunoprecipitation andWestern blotting, namely with the A structural subunit of PP2A (PP2A A), the structure-specific recognition protein 1 (SSRP1, a component of the facilitate chromatin transcription (FACT) complex), and a new form of the transcription factor EC (TFEC). Thus, tEBNA-LP appears to be involved not only in cell resistance to apoptosis through its interaction with two PP2A subunits, but also in other processes where its ability to co-activate transcriptional regulators could be important. [ABSTRACT FROM AUTHOR]
- Published
- 2018
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