Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1

Journal of Virology
M R HicksA J Sinclair

Abstract

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.

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Citations

Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Patrice MorandCarlo Petosa
Aug 17, 2004·Journal of Virology·Michelle J WestDerek N Woolfson
Mar 29, 2014·Clinical Microbiology and Infection : the Official Publication of the European Society of Clinical Microbiology and Infectious Diseases·M A LorenzettiM V Preciado
Mar 13, 2014·Journal of Medical Virology·Ying YangBing Luo
Feb 18, 2006·Molecular Cell·Carlo PetosaChristoph W Müller
Jan 1, 2012·Pathogens·Stelios Tzellos, Paul J Farrell
Jul 18, 2003·The Journal of General Virology·Alison J Sinclair
Jul 18, 2008·Biochemical Society Transactions·Questa H KarlssonAlison J Sinclair

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