Epstein-Barr virus glycoprotein gL (gL)

Epstein-Barr virus (EBV) glycoprotein gL is a critical component of the viral entry machinery, forming a stable non-covalent heterodimeric complex with glycoprotein H (gH) (UniProt: P03212). This gH/gL complex is essential for EBV to infect both B lymphocytes and epithelial cells, where gL acts as a molecular chaperone required for the correct folding and trafficking of gH to the viral envelope (PubMed: 30651331). In B cell infection, the gH/gL complex associates with the accessory protein gp42 to bind HLA class II molecules, while in epithelial cells, it interacts directly with host integrins to trigger membrane fusion (PubMed: 29311413). Because of its indispensable role in mediating viral access to host cells and its high conservation, gL is a primary target for the development of neutralizing antibodies and prophylactic vaccines. Experimental therapies, such as the monoclonal antibody AMMO1, target the gH/gL interface to potently inhibit infection across multiple cell types (PubMed: 29311413). Current clinical research focuses on using gH/gL-based immunogens to prevent EBV-associated malignancies and infectious mononucleosis (NIH/NIAID).

Other names

BKRF2Envelope glycoprotein LEBV gLEpstein-Barr virus BKRF2

Neutralization of viral entry by blocking the gH/gL complex interaction with host cell membranes or preventing the formation of the fusion-triggering complex.