The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH. Fusion of EBV with B-lymphocytes requires the additional receptor-binding protein gp42, which forms a complex with gH/gL. The heterodimer gH/gL targets also host EPHA2 to promote viral entry. Interacts with glycoprotein H (gH); this interaction is necessary for the correct processing and cell surface expression of gH. The heterodimer gH/gL seems to interact with gB trimers during fusion. The heterodimer gH/gL interacts with host EPHA2 to facilitate virus internalization and fusion. gL associates with the extravirion surface through its binding to gH. During virion morphogenesis, this protein probably accumulates in the host trans-Golgi where secondary envelopment occurs. Belongs to the herpesviridae glycoprotein L family.