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The HLA-presented adenovirus hexon protein peptide epitope is a molecular complex formed by the association of a viral peptide fragment with a Human Leukocyte Antigen (HLA) molecule on the surface of infected cells. The hexon protein is the most abundant structural protein of the adenovirus capsid and is a primary target for the host adaptive immune response due to its highly conserved sequences across different adenovirus serotypes [1, 2]. During the viral life cycle, hexon proteins are processed by the host cell proteolytic machinery into short peptides, typically 8-11 amino acids long, which are then loaded onto MHC Class I or Class II molecules [1]. These complexes are subsequently presented on the cell surface, where they serve as the primary ligands for T-cell receptors (TCRs) on CD8+ and CD4+ T cells [4]. Recognition of these epitopes by the immune system is essential for the clearance of adenovirus infections, making them a focal point for therapeutic intervention. In clinical practice, these epitopes are targeted using adoptive virus-specific T-cell (VST) therapies, which are particularly vital for treating life-threatening adenovirus infections in immunocompromised patients, such as those undergoing hematopoietic stem cell transplantation [3, 4]. Furthermore, these peptide-HLA complexes are being utilized in the design of next-generation vaccines and TCR-engineered cellular therapies to provide broad protection against multiple adenovirus strains [1].
Recognition by T-cell receptors (TCRs) on cytotoxic T lymphocytes, leading to the targeted lysis of infected host cells.
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