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Human cytomegalovirus (HCMV) antigens pp65 (UL83) and gB (UL55) are two of the most immunodominant proteins of the virus and serve as primary targets for vaccine and immunotherapy development. pp65 is a major tegument phosphoprotein that is essential for subverting the host's innate immune response by inhibiting the cGAS/STING and IFI16 DNA-sensing pathways, while also acting as a principal target for cytotoxic T-lymphocyte (CTL) responses [1, 12, 13]. Glycoprotein B (gB) is a class III viral fusion protein located on the viral envelope that is critical for viral entry into host cells and cell-to-cell spread, making it the primary target for neutralizing antibodies [7, 9, 15]. These antigens are frequently combined in multi-antigen vaccine candidates, such as the DNA vaccine ASP0113, to elicit both cellular and humoral immunity [6, 9]. Beyond their role in viral infection, pp65 and gB are notably expressed in glioblastoma multiforme (GBM) tumor cells, where they are utilized as 'foreign' targets for dendritic cell vaccines and adoptive T-cell therapies to induce anti-tumor immune responses [1, 3, 5].
Induction of antigen-specific CD4+ and CD8+ T-cell responses (pp65) and production of neutralizing antibodies (gB) to prevent viral entry and replication.
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