Envelope glycoprotein E (Herpes simplex virus type 2) (gE)

Envelope glycoprotein E (gE) is a type I transmembrane protein of Herpes Simplex Virus type 2 (HSV-2) that plays a dual role in viral pathogenesis and immune evasion (UniProt P06487). It forms a functional heterodimer with glycoprotein I (gI), which is essential for the efficient cell-to-cell spread of the virus, particularly within the nervous system and across epithelial junctions, by facilitating viral transport to cell-cell contacts (PubMed: 10482573). Beyond its structural roles, the gE-gI complex functions as a viral Fc gamma receptor (vFcγR) that binds the Fc region of host IgG antibodies. This binding mediates a process known as antibody bipolar bridging, which effectively shields the virus and infected cells from host immune effector functions such as complement activation and antibody-dependent cellular cytotoxicity (ADCC) (PubMed: 28250123). Due to its critical involvement in both dissemination and immune shielding, gE is a primary target for next-generation HSV-2 vaccines, including mRNA and recombinant subunit candidates like GSK3943104A and BNT163 (GSK Pipeline; BioNTech). These therapeutic strategies aim to elicit antibodies that both neutralize viral spread and block the immune-evasive properties of the protein to prevent or treat genital herpes.

Other names

Glycoprotein EgEUS8HSV-2 gEgE2

Induction of neutralizing antibodies that inhibit viral cell-to-cell spread and blocking of the viral Fc gamma receptor to prevent immune evasion and enhance antibody-dependent cellular cytotoxicity (ADCC).