Epstein-Barr virus glycoprotein 42 (gp42)

Epstein-Barr virus glycoprotein 42 (gp42) is a multifunctional, type II membrane envelope protein essential for EBV entry into B lymphocytes. It contains a flexible N-terminal domain that binds to the viral gH/gL complex and a C-terminal C-type lectin-like domain (CTLD) that specifically binds to the B cell receptor, human leukocyte antigen (HLA) class II. Gp42 acts by forming a complex with gH/gL, then engaging HLA class II on B cells, which in turn triggers conformational changes that activate the viral fusion machinery, ultimately leading to membrane fusion and viral entry. Structural studies show important functional regions: the gH/gL interaction site within residues 36–81 of the N-terminus and the HLA binding site within the C-terminal CTLD (residues 94–221). Gp42 is unique to EBV and is strictly required for B cell infection, though not for epithelial cell entry. Peptides and antibodies derived against gp42 can block B cell infection, suggesting gp42 is a potentially valuable therapeutic and diagnostic target.

Other names

EBV gp42glycoprotein 42gp42 protein

Targeting gp42 with inhibitory peptides or antibodies blocks its interaction with gH/gL or HLA class II, thereby preventing B cell fusion and EBV entry