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The Varicella-zoster virus (VZV) glycoprotein complex is a group of essential proteins located on the viral envelope, including gB, gC, gE, gH, gI, gK, gL, gM, and gN, which are critical for the virus's ability to infect host cells and spread within the body (PMID: 26903605). These glycoproteins function in a coordinated manner to facilitate viral attachment, mediate the fusion of the viral envelope with host cell membranes, and enable efficient cell-to-cell transmission, which is a defining characteristic of VZV pathogenesis (UniProt: P09333). Glycoprotein E (gE) is the most prominently expressed and is a major target for the host immune system, serving as the primary antigen in the recombinant zoster vaccine (Shingrix) to elicit protective T-cell and antibody responses (PMID: 29198119). Other complexes, such as gH/gL, are part of the core fusion machinery required for entry into various cell types, including keratinocytes and neurons (PMID: 25100805). Therapeutic interventions targeting these glycoproteins include both live-attenuated and subunit vaccines for the prevention of chickenpox and shingles, as well as immune globulins for post-exposure prophylaxis in vulnerable populations (CDC: Varicella Vaccination). Understanding these complexes is vital for managing VZV-related diseases and their complications, such as postherpetic neuralgia and vasculopathy.
Vaccines induce active immunity by presenting VZV glycoproteins (e.g., gE) to the immune system, leading to the production of neutralizing antibodies and virus-specific T-cells; immune globulins provide immediate, passive neutralization of the virus by binding to these surface glycoproteins (PMID: 26903605).
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