Varicella-zoster virus (VZV) serves as the prototype for the alphaherpesvirus subgroup, classified under the Varicellovirus genus. The VZV genome encodes a minimum of six glycoproteins: gB, gC, gE, gH, gI, and gL. Among these, gE (formerly known as gpI or gp98) is the most abundant in the virion envelope and is the primary glycoprotein present on the surface of infected cells.
VZV gE is a classic type I transmembrane glycoprotein, extensively modified by N-linked and O-linked glycosylation, sialylation, and sulfation. It also features a phosphorylation site for serine/threonine casein kinase II. Additionally, gE has the capacity to form homodimers that undergo tyrosine phosphorylation.
During infection, VZV gE interacts with VZV gI to form a protein complex. Notably, gE on the surface of infected cells has been identified as an Fc receptor for nonimmune IgG. Homology studies indicate that gE exhibits structural characteristics akin to those of several nonviral cell surface receptors, such as the Fc receptor (FcγRII) and the low-density lipoprotein (LDL) receptor.