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Cancers 2018, 10(1), 12; doi:10.3390/cancers10010012

New Interactors of the Truncated EBNA-LP Protein Identified by Mass Spectrometry in P3HR1 Burkitt’s Lymphoma Cells

1
UMR 8126 CNRS, Univ. Paris-Sud, Université Paris-Saclay, Institut Gustave Roussy, F-94805 Villejuif, France
2
Proteomic Platform, Institut Gustave Roussy, Villejuif F-94805, France
3
Laboratoire de Génétique Oncologique, Ecole Pratique des Hautes Etudes, F-75014 Paris, France
4
UMR 1186 Inserm, Univ. Paris-Sud, EPHE, Université Paris-Saclay, Institut Gustave Roussy, F-94805 Villejuif, France
Deceased.
*
Author to whom correspondence should be addressed.
Received: 16 November 2017 / Revised: 21 December 2017 / Accepted: 21 December 2017 / Published: 5 January 2018
(This article belongs to the Special Issue Epstein–Barr Virus Associated Cancers)
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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 3′ 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 and Western 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. View Full-Text
Keywords: EBV; Wp-restricted latency; mass spectrometry; EBNA-LP; PP2A; SSRP1; TFEC EBV; Wp-restricted latency; mass spectrometry; EBNA-LP; PP2A; SSRP1; TFEC
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Chelouah, S.; Cochet, E.; Couvé, S.; Balkaran, S.; Robert, A.; May, E.; Ogryzko, V.; Wiels, J. New Interactors of the Truncated EBNA-LP Protein Identified by Mass Spectrometry in P3HR1 Burkitt’s Lymphoma Cells. Cancers 2018, 10, 12.

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