Herpes simplex virus glycoprotein E (gE)

Herpes simplex virus glycoprotein E (gE) is a type I transmembrane protein located in the viral envelope of both HSV-1 and HSV-2. It forms a functional heterodimer with glycoprotein I (gI), which serves as a viral Fc gamma receptor (vFcγR) that binds the Fc domain of host immunoglobulin G (IgG) [1]. This binding mechanism facilitates "antibody bipolar bridging," allowing the virus to evade host immune responses by preventing complement-mediated neutralization and antibody-dependent cellular cytotoxicity (ADCC) [2][3]. Additionally, the gE/gI complex is crucial for the efficient cell-to-cell spread of the virus, particularly within the nervous system and polarized epithelial tissues, by facilitating the sorting of viral components to cell junctions [4]. Because of its dual role in immune evasion and viral transmission, gE is a major target for therapeutic interventions, including monoclonal antibodies like HDIT101 and multi-antigen subunit vaccines [5]. Targeting gE aims to reduce the frequency of viral reactivation, limit lesion formation, and decrease the risk of transmission to uninfected partners [6]. Sources: [1] UniProt (P04488); [2] Ndjamen et al. (2014) J. Virol.; [3] Hook et al. (2019) Vaccine; [4] Johnson et al. (2001) J. Virol.; [5] ClinicalTrials.gov (NCT04161963); [6] Awasthi et al. (2017) PLoS Pathogens.

Other names

Envelope glycoprotein EUS8HSV gEgE/gI complex

Inhibition of viral cell-to-cell spread and blockade of IgG Fc-mediated immune evasion