Little is known about Epstein Barr Virus (EBV) proteins that participate in viral DNA cleavage and packaging. Genes encoding potential terminase subunit and portal protein homologs include BGRF1/BDRF1, BALF3, BFRF1A and BBRF1 respectively. EBV mutants with deletions in one or more of these genes were impaired for DNA packaging (Pavlova et al., 2013). In the current study, BBRF1 oligomers were purified from recombinant baculovirus infected insect cell extracts. Transmission electron microscopy revealed that purified EBV portals retained features typically found in other portals including a central channel with clip, stem and wing/crown domains. Although compounds have been identified that target DNA encapsidation in human cytomegalovirus, herpes simplex viruses and varicella-zoster virus, the identification of new EBV targets has lagged significantly. Characterization of the EBV portal will direct studies aimed at developing potential small molecular inhibitors of the EBV encapsidation process.,Copyright © 2019. Published by Elsevier Inc.