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Journal of Virology, November 2005, p. 13822-13828, Vol. 79, No. 21
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.21.13822-13828.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Mutation of a Single Amino Acid Residue in the Basic Region of the Epstein-Barr Virus (EBV) Lytic Cycle Switch Protein Zta (BZLF1) Prevents Reactivation of EBV from Latency

Celine Schelcher,^1, Sarah Valencia,^1,, Henri-Jacques Delecluse,² Matthew Hicks,^1, and Alison J. Sinclair^1*

Biochemistry Department, School of Life Sciences, University of Sussex, Brighton BN1 9QG, United Kingdom,¹ Applied Tumour Virology, German Cancer Centre, Im Neuenheimer Feld 242, 69120, Heidelberg, Germany²

Received 20 May 2005/ Accepted 5 August 2005

Zta, the product of the BZLF1 gene carried by Epstein-Barr virus (EBV), is crucial for reactivation of EBV from latency. Zta is a member of the bZIP family of transcription factors, and in common with many of these, Zta possesses a conserved cysteine residue in its basic region (C189) and a further cysteine residue in its ZIP region (C222). We demonstrate that C189 is required to reactivate EBV from latency but C222 is not and that this single amino acid affects two independent functions of Zta, (i) binding to a Zta-responsive site and (ii) manipulating the cell cycle.

Celine Schelcher and Sarah Valencia contributed to this work equally.

Present address: GSF, Institute for Clinical Molecular Biology and Tumor Genetics, D-81377 Munich, Germany.

Present address: School of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom.

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