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Epstein–Barr virus glycoprotein H (**gH**) is a **core envelope glycoprotein** essential for the membrane fusion process that enables EBV entry into host B lymphocytes and epithelial cells[1][2][5][3]. It **forms a heterodimeric complex with glycoprotein L (gL)**, acting together as part of a multi-component fusion apparatus with glycoprotein B (gB) and, in B cells, accessory glycoprotein gp42[1][2][3][5][6][7]. The gH/gL complex enables viral penetration by **regulating attachment to host cell receptors (including integrins for epithelial cells and HLA class II via gp42 for B cells)**, and is a major determinant of cell tropism[1][2][6]. Mutations in gH disrupt membrane fusion and compromise infection[3][7]. Although there are no current drugs that directly target EBV gH in clinical use, the fusion complex is a **potential therapeutic target for antiviral entry inhibitors or neutralizing antibody approaches**[5][6].
Inhibition of viral entry (theoretical/experimental, by blocking gH/gL complex function); Neutralization of membrane fusion (by antibody or hypothetical small molecule/blocker)
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