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Updated: Aug 11, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein
M R Hicks1, S Balesaria, C Medina-Palazon
1School of Biological Sciences, School of Biological Sciences, University of Sussex, Brighton, East Sussex BN1 9QG, United Kingdom.
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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