This recombinant HHV-2 Envelope glycoprotein E protein is produced using a cell-free in vitro expression system in E.coli. The protein encompasses the full length of the mature form. Cell-free systems utilize extracts from whole cells, capable of transcribing, translating, and post-translationally modifying the recombinant protein. These extracts contain all the necessary molecules and enzymes. With the addition of cofactors, Envelope glycoprotein E proteins can be synthesized within a few hours. However, this system may not be suitable for large-scale protein production. Notable advantages of this system include the ability to synthesize proteins without cell culturing, and the capacity to express multiple proteins simultaneously.
HSV-2 gE plays a crucial role in cell-to-cell transmission and virus-induced cell fusion. It acts as an immune evasion molecule by binding to the IgG Fc domain. HSV-2 gE collaborates with gC to protect the virus from antibody and complement neutralization. Immunization with gE generates antibodies that prevent gE-mediated IgG Fc binding and cell-to-cell dissemination. Consequently, gE holds potential as an antigen for inclusion in a multivalent subunit vaccine designed to counteract HSV-2 immune evasion.