Identification of Epstein-Barr Virus Replication Proteins in Burkitt’s Lymphoma Cells

Pathogens

Chris Traylen²  Sharada Ramasubramanyan²  Jianmin Zuo³  Martin Rowe³  Rajaei Almohammad²  Kate Heesom⁴  Steve M. M. Sweet¹  David A. Matthews⁵  Alison J. Sinclair² 

[1] Genome Damage and Stability Centre, University of Sussex, Brighton BN1 9RQ, UK; E-Mail:;School of Life Sciences, University of Sussex, Brighton BN1 9QG, UK; E-Mails:;School of Cancer Sciences and Centre for Human Virology, University of Birmingham College of Medical and Dental Sciences, Edgbaston, Birmingham B15 2TT, UK; E-Mails:;University of Proteomics Facility, Biomedical Sciences Building, Bristol BS8 1TD, UK; E-Mail:;School of Cellular and Molecular Medicine, University of Bristol, Biomedical Sciences Building, Bristol BS8 1TD, UK; E-Mail:

关键词: virus;    cancer;    replication;    proteome;    herpes;    Epstein-Barr;   

DOI  :  10.3390/pathogens4040739

来源: mdpi

【 摘 要 】

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 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.

【 授权许可】

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.