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Varicella-zoster virus glycoprotein E (gE) is the most abundant and immunogenic surface protein of the Varicella-zoster virus (VZV), a member of the Alphaherpesvirinae subfamily [1]. It is essential for viral replication, facilitating both the initial infection of host cells and the subsequent cell-to-cell spread of the virus through the formation of syncytia [2]. Beyond its structural role, gE acts as a viral Fc receptor, binding the Fc portion of host IgG to potentially interfere with immune effector functions and facilitate immune evasion [1]. In clinical practice, gE serves as the primary antigenic component in recombinant subunit vaccines designed to prevent herpes zoster (shingles) and postherpetic neuralgia [3]. By presenting this protein to the immune system, vaccines like Shingrix trigger the production of high-titer neutralizing antibodies and the expansion of VZV-specific CD4+ T cells [3][5]. This dual immune activation is crucial for maintaining long-term protection against the reactivation of latent VZV in sensory ganglia, particularly in aging or immunocompromised populations [4].
Induction of active immunity through the stimulation of VZV-specific humoral (antibody) and cell-mediated immune responses, primarily targeting the gE surface protein to prevent viral entry and spread [3][4].
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