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Cytomegalovirus (CMV) phosphoprotein 150 (pp150), encoded by the UL32 gene, is a major tegument protein essential for the stabilization of the viral capsid during maturation and egress (UniProt P06473). In infected cells, pp150 and other viral proteins like pp65 and IE1 are processed into short peptides and presented on the cell surface by Human Leukocyte Antigen (HLA) class I molecules. This peptide-HLA complex serves as a critical target for the host's immune system, specifically for CD8+ cytotoxic T-lymphocytes (CTLs), which recognize these epitopes to eliminate infected cells (PubMed: 31110034). Therapeutic strategies targeting these complexes include adoptive cell transfer of CMV-specific T-cells and the development of TCR-engineered T-cells (TCR-T) designed to recognize specific pp150 epitopes, such as those presented by HLA-A*02:01. Additionally, multi-antigen vaccines like Triplex utilize pp150 to induce robust cellular immunity in transplant recipients (PubMed: 28655821). These interventions are primarily aimed at preventing or treating CMV-related complications in immunocompromised individuals, such as hematopoietic stem cell or solid organ transplant recipients. By enhancing the cellular immune response against these viral antigens, these therapies help control viral replication and reduce the risk of clinical CMV disease.
Recognition of the viral peptide-HLA complex by the T-cell receptor (TCR) on CD8+ cytotoxic T-lymphocytes, triggering the release of perforin and granzymes to induce apoptosis in CMV-infected cells.
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