Functional interaction between Epstein-Barr virus replication protein Zta and host DNA damage response protein 53BP1

Bailey, Sarah G, Verrall, Elizabeth, Schelcher, Celine, Rhie, Alex, Doherty, Aidan J and Sinclair, Alison J (2009) Functional interaction between Epstein-Barr virus replication protein Zta and host DNA damage response protein 53BP1. Journal of Virology, 83 (21). pp. 11116-11122. ISSN 0022-538X

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Abstract

Epstein-Barr virus (EBV; human herpesvirus 4) poses major clinical problems worldwide. Following primary infection, EBV enters a form of long-lived latency in B lymphocytes, expressing few viral genes, and it persists for the lifetime of the host with sporadic bursts of viral replication. The switch between latency and replication is governed by the action of a multifunctional viral protein Zta (also called BZLF1, ZEBRA, and Z). Using a global proteomic approach, we identified a host DNA damage repair protein that specifically interacts with Zta: 53BP1. 53BP1 is intimately connected with the ATM signal transduction pathway, which is activated during EBV replication. The interaction of 53BP1 with Zta requires the C-terminal ends of both proteins. A series of Zta mutants that show a wild-type ability to perform basic functions of Zta, such as dimer formation, interaction with DNA, and the transactivation of viral genes, were shown to have lost the ability to induce the viral lytic cycle. Each of these mutants also is compromised in the C-terminal region for interaction with 53BP1. In addition, the knockdown of 53BP1 expression reduced viral replication, suggesting that the association between Zta and 53BP1 is involved in the viral replication cycle.

Item Type: Article
Additional Information: Main author, majority of research undertaken my my research group. Collaboration for reagents with another group at University of Sussex.
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science
Depositing User: Sarah Georgina Bailey
Date Deposited: 06 Feb 2012 19:38
Last Modified: 29 Oct 2012 10:40
URI: http://sro.sussex.ac.uk/id/eprint/21548
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