The Epstein-Barr virus (EBV) immediate-early protein BRLF1 is a transcripti
onal activator that mediates the switch from latent to lytic viral replicat
ion. Many transcriptional activators function, in part, due to an interacti
on with histone acetylases, such as CREB-binding protein (CBP). Were we dem
onstrate that BRLF1 interacts with the amino and carboxy termini of CBP and
that multiple domains of the BRLF1 protein are necessary for this interact
ion. Furthermore, we show that the interaction between BRLF1 and CBP is imp
ortant for BRLF1-induced activation of the early lytic EBV gene SM in Raji
cells.