Traylen, Chris, Ramasubramanyan, Sharada, Zuo, Jianmin, Rowe, Martin, Almohammad, Rajei, Heesom, Kate, Sweet, Steve M M, Matthews, David and Sinclair, Alison J (2015) Identification of Epstein-Barr virus replication proteins in Burkitt’s lymphoma cells. Pathogens, 4 (4). pp. 739-751. ISSN 2076-0817

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Abstract

The working model to describe the mechanisms used to replicate the cancer-associated virus Epstein-Barr virus (EBV) is partly derived from comparisons with other members of the Herpes virus family. Many genes within the EBV genome are homologous across the herpes virus family. Published transcriptome data for the EBV genome during its lytic replication cycle show extensive transcription, but the identification of the proteins is limited. We have taken a global proteomics approach to identify viral proteins that are expressed during the EBV lytic replication cycle. We combined an enrichment method to isolate cells undergoing EBV lytic replication with SILAC-labeling coupled to mass-spectrometry and identified viral and host proteins expressed during the OPEN ACCESS Pathogens 2015, 4 740 EBV lytic replication cycle. Amongst the most frequently identified viral proteins are two components of the DNA replication machinery, the single strand DNA binding protein BALF2, DNA polymerase accessory protein BMRF1 and both subunits of the viral ribonucleoside-diphosphate reductase enzyme (BORF2 and BaRF1). An additional 42 EBV lytic cycle proteins were also detected. This provides proteomic identification for many EBV lytic replication cycle proteins and also identifies post-translational modifications.

Item Type:	Article
Keywords:	Virus, silac, proteomics, cancer
Schools and Departments:	School of Life Sciences > Biochemistry School of Life Sciences > Sussex Centre for Genome Damage and Stability
Subjects:	Q Science Q Science > QR Microbiology Q Science > QR Microbiology > QR0355 Virology
Depositing User:	Alison Sinclair
Date Deposited:	30 Oct 2015 09:24
Last Modified:	07 Mar 2017 08:11
URI:	http://srodev.sussex.ac.uk/id/eprint/57421

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