CMV-derived peptide–major histocompatibility complex class I complex

CMV-derived peptide–major histocompatibility complex class I complexes are formed when peptides processed from cytomegalovirus proteins are loaded onto MHC class I molecules within infected host cells and presented at the cell surface[1][2]. These complexes are recognized by the T cell receptor (TCR) of CD8+ cytotoxic T cells, which can trigger immune-mediated killing of the infected cell. CMV encodes various immune evasion proteins that manipulate the antigen processing and presentation pathway to reduce the display of these peptide–MHC complexes, assisting the virus in escaping immune detection[1][4]. In therapeutic contexts, these complexes serve as targets for adoptive T cell transfer or engineered TCR therapies, particularly in immunocompromised patients or after hematopoietic stem cell transplantation. Monitoring the abundance or recognition of these complexes also provides important biomarkers for immune surveillance and efficacy of antiviral immunity[5].

Other names

CMV peptide-MHC complexCMV antigen–MHC class I complexcytomegalovirus peptide–MHC complex

T cell receptor (TCR)–mediated cytotoxicity: T cells recognize the CMV peptide–MHC complex, leading to targeted cell killing[2][5]. Modulation by viral immune evasion proteins (e.g., HCMV US proteins interfere with peptide presentation)[4].