Epstein-Barr virus is a ubiquitous orally-transmitted human herpesvirus that is carried by most of the adult population. It establishes latent infections in B lymphocytes, reactivates periodically from latency and can be amplified in epithelial cells where it is thought more commonly to undergo lytic replication. Entry into either cell involves fusion of the virus envelope with a cell membrane. Fusion with a B cell requires four envelope glycoproteins, gB and a ternary complex of gHgLgp42. Fusion is triggered by an interaction between gp42 and HLA class II. Fusion with an epithelial cell requires three envelope glycoproteins, gB and a binary complex of gHgL. The presence of gp42 blocks infection and blocks the interaction of gHgL with a specific receptor on the epithelial cell surface. We recently demonstrated that both integrins αvβ6 and αvβ8 can serve as specific receptors for gHgL and that on binding to gHgL, even in a soluble form, can provide the trigger for direct virus fusion with the epithelial cell plasma membrane. It reveals yet another way in which an integrin can be used by a pathogen to invade a cell.