The BDLF2 protein of Epstein-Barr virus is a type II glycosylated envelope protein whose processing is dependent on coexpression with the BMRF2 protein.

Epstein-Barr virus has been documented to encode for ten envelope glycoproteins, gB, gH, gL, gM, gN, gp350, gp42, gp78, gp150 and BMRF2. The BDLF2 open reading frame is also predicted to encode a type II membrane protein but, although found in the virion, it has been described as a component of the tegument. We show here that, as predicted, it is the eleventh envelope glycoprotein of the virus. The full length 65 kDa glycoprotein formed a complex with BMRF2 and, as its homologs in other gammaherpesviruses, was dependent on BMRF2, for authentic processing and transport. Two cleavage products of BDLF2 were also identified in cells and in purified virion particles, one corresponding approximately to the aminoterminal half of the protein, that remained associated with the full length form, and one corresponding to the carboxyterminal glycosylated portion of the protein which did not.