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Adenovirus peptide-MHC complexes are composite molecular structures formed when short peptides derived from adenoviral proteins are bound within the peptide-binding groove of host Major Histocompatibility Complex (MHC) molecules. These complexes are displayed on the surface of infected cells, serving as the primary signal for recognition by the adaptive immune system, specifically by T-cell receptors (TCRs) on CD8+ and CD4+ T cells (1.2.1, 1.2.4). The most common adenoviral antigens involved include the major capsid protein hexon, as well as penton base and fiber proteins (1.1.2, 1.1.4). In immunocompromised individuals, such as those undergoing hematopoietic stem cell transplantation, the failure of the immune system to recognize these complexes can lead to severe, life-threatening adenovirus infections (1.3.1, 1.5.1). Consequently, these complexes are critical therapeutic targets for adoptive T-cell therapies, such as virus-specific T cells (VSTs), which are selected or engineered to recognize and eliminate cells presenting these viral antigens (1.3.3, 1.3.4). Some adenovirus serotypes attempt to evade this immune detection by synthesizing proteins like E3-19K, which sequester MHC molecules in the endoplasmic reticulum to prevent their surface expression (1.2.2, 1.4.3).
T-cell receptor (TCR) recognition and binding to the peptide-MHC complex, which triggers the activation of cytotoxic T-lymphocytes (CTLs) and subsequent lysis of the infected cell.
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