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Journal of Virology, June 2001, p. 5381-5384, Vol. 75, No. 11
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.11.5381-5384.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Biophysical Analysis of Natural Variants of the Multimerization Region of Epstein-Barr Virus Lytic-Switch Protein BZLF1

Matthew R. Hicks,1 Sara Balesaria,1 Cahora Medina-Palazon,1 Maya J. Pandya,1,2 Derek N. Woolfson,1,2 and Alison J. Sinclair1,*

School of Biological Sciences1 and Centre for Biomolecular Design and Drug Development,2 School of Biological Sciences, University of Sussex, Brighton, East Sussex BN1 9QG, United Kingdom

Received 6 December 2000/Accepted 26 February 2001

BZLF1 plays a key role in the induction of Epstein-Barr virus (EBV) replication. On the basis of limited sequence homology and mutagenesis experiments, BZLF1 has been described as a member of the bZip family of transcription factors, but this prospect has not been rigorously tested to date. Here, we present biophysical analysis of the multimerization domain of BZLF1, from three natural variants of EBV, and demonstrate for the first time that the region between amino acids 196 and 227 is sufficient to direct folding as a coiled-coil dimer in vitro.

* Corresponding author. Mailing address: School of Biological Sciences, University of Sussex, Brighton, E. Sussex BN1 9QG, United Kingdom. Phone: (44) 1273 678 194. Fax: (44) 1273 678 433. E-mail: a.j.sinclair{at}Sussex.ac.uk.

Journal of Virology, June 2001, p. 5381-5384, Vol. 75, No. 11
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.11.5381-5384.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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