Epstein-Barr virus gp42 envelope glycoprotein (gp42)

The Epstein-Barr virus (EBV) gp42 envelope glycoprotein is a critical component of the viral entry machinery, specifically required for the infection of B lymphocytes (UniProt: P03209). It functions as part of a heterotrimeric complex with glycoproteins gH and gL, where gp42 acts as the receptor-binding subunit that recognizes HLA class II molecules on the surface of B cells (Sathiyamoorthy et al., 2017). This interaction triggers a conformational change in the gH/gL complex, which in turn activates the fusion protein gB to mediate viral-host membrane fusion. Interestingly, gp42 also serves as a tropism switch; while it is essential for B-cell entry, its presence inhibits the infection of epithelial cells, which require only the gH/gL complex (Borza & Hutt-Fletcher, 2002). Given its indispensable role in B-cell infection—the primary site of EBV latency—gp42 is a high-priority target for the development of prophylactic vaccines and therapeutic neutralizing antibodies. Current research focuses on blocking the gp42-MHC II interface to prevent the establishment of EBV infection and its associated malignancies, such as Burkitt lymphoma and nasopharyngeal carcinoma (Bu et al., 2019).

Other names

BZLF2Glycoprotein 42EBV gp42Epstein-Barr virus glycoprotein gp42

Neutralizing antibodies or vaccines target gp42 to block its interaction with HLA class II receptors on B cells, thereby preventing viral entry and subsequent infection (Sathiyamoorthy et al., 2017). Some agents may also interfere with the formation of the gH/gL/gp42 complex or the triggering of the gB fusion protein (Bu et al., 2019).