Human Major Histocompatibility Complex class I and II peptide-binding grooves presenting Cytomegalovirus pp65 epitopes (HLA-CMV pp65 complex)

The Human Major Histocompatibility Complex (MHC) class I and II peptide-binding grooves presenting Cytomegalovirus (CMV) pp65 epitopes are essential structures for the cellular immune recognition of CMV (PubMed: 15140031). The pp65 protein, encoded by the UL83 gene, is the most immunodominant antigen of CMV and is the primary target for both CD8+ and CD4+ T-cell responses (PubMed: 10438932). MHC class I molecules (HLA-A, B, and C) present pp65-derived peptides, such as the widely studied NLVPMVATV epitope, to cytotoxic T lymphocytes to trigger the lysis of infected cells (Journal of Virology: 10.1128/JVI.73.10.8706-8712.1999). MHC class II molecules (HLA-DR, DQ, and DP) present epitopes to helper T cells, which are crucial for maintaining long-term immunity and coordinating the overall antiviral response (Blood: 10.1182/blood-2017-02-768564). This target complex is a focal point for the development of adoptive T-cell therapies and vaccines, particularly for immunocompromised patients, such as hematopoietic stem cell or solid organ transplant recipients, who are at high risk for CMV reactivation (NCBI: NBK27156). Therapeutic strategies involve the infusion of ex vivo expanded CMV-specific T cells or the use of viral vectors to stimulate endogenous T cells that recognize these specific pMHC complexes.

Other names

HLA-peptide complexCMV pp65-HLA complexpMHC-CMV pp65UL83-derived peptide-MHC complexCMV antigen-presenting complex

Recognition of the peptide-MHC complex by specific T-cell receptors (TCRs) leads to the activation, proliferation, and effector function of CMV-specific T lymphocytes, resulting in the elimination of CMV-infected cells.