Epstein-Barr virus glycoprotein 350, glycoprotein H, glycoprotein L, and glycoprotein 42 (gp350, gH, gL, and gp42)

Epstein-Barr virus glycoproteins gp350, gH, gL, and gp42 are essential viral envelope proteins required for host cell entry. gp350 is the major attachment glycoprotein that binds to the complement receptor CR2 (CD21) on B cells, facilitating the initial attachment of EBV to host cells. gH and gL form a tightly associated heterodimer that regulates the membrane fusion step necessary for viral entry into both B cells and epithelial cells, with gH/gL interacting directly with both viral glycoprotein B (gB) and host integrins. gp42 acts as a tropism-switching protein allowing infection of B cells by engaging HLA class II on the cell surface and triggering fusion in cooperation with the gH/gL complex. Together, these glycoproteins constitute the minimal fusion and attachment machinery for EBV, and each plays a critical role in host range, cell tropism, and immune modulation. Due to their central role in viral entry, they are considered important antiviral and vaccine targets, but pose significant challenges due to antigenic variability and immune evasion strategies of the virus.

Other names

BLLF1major envelope glycoproteinglycoprotein HBGLF2glycoprotein LBLLF2BZLF2envelope glycoprotein 42

Inhibition of viral entry by blocking receptor binding (gp350), prevention of envelope fusion with host cell membranes by disrupting the gH/gL/gp42 machinery, and neutralization of virus by inducing antibodies that prevent glycoprotein-mediated infection.