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The Cytomegalovirus (CMV) phosphoprotein 65 (pp65), also known as UL83, is the primary tegument protein of Human Cytomegalovirus and serves as the immunodominant target for the host's cellular immune response. During infection, pp65 is processed by the proteasome into short peptides, such as the well-characterized NLVPMVATV decamer, which are then loaded onto MHC class I molecules (typically HLA-A*02:01) and presented on the cell surface. This peptide-MHC (pMHC) complex is specifically recognized by the T-cell receptors (TCRs) of CD8+ cytotoxic T-lymphocytes, triggering the destruction of infected cells. In clinical medicine, this complex is a critical therapeutic target for the development of adoptive T-cell therapies (VSTs), TCR-engineered T-cells, and peptide-based vaccines aimed at controlling CMV reactivation in immunocompromised transplant recipients. Furthermore, because pp65 expression has been detected in certain malignancies like glioblastoma, the pp65-pMHC complex is also being investigated as a target for cancer immunotherapy.
T-cell receptor (TCR) binding, T-cell mediated cytotoxicity, Active immunization
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