Epstein–Barr virus peptide-MHC class I complex (EBV pMHC-I)

The Epstein–Barr virus (EBV) peptide-MHC class I complex is a molecular assembly consisting of EBV-derived antigenic peptides bound to Major Histocompatibility Complex (MHC) class I molecules on the surface of infected cells (NIH, 2019). This complex serves as the primary signal for recognition and elimination of EBV-infected cells by CD8+ cytotoxic T lymphocytes (CTLs) (Pudney et al., 2005). In healthy individuals, this interaction maintains viral latency and prevents disease; however, in immunocompromised patients or through viral immune evasion, the failure of this recognition can lead to EBV-associated malignancies such as post-transplant lymphoproliferative disorder (PTLD) and nasopharyngeal carcinoma (Raab-Traub, 2015). Therapeutic strategies targeting these complexes include adoptive T-cell therapies, such as the approved allogeneic product tabelecleucel, and investigational T-cell receptor (TCR)-engineered T cells (EMA, 2022; Jo et al., 2023). These therapies utilize specific TCRs to bind the pMHC complex, triggering the release of perforin and granzymes to induce apoptosis in the target cell (Patsnap, 2024). Additionally, EBV peptide vaccines are being developed to enhance the endogenous presentation and recognition of these complexes (WithPower, 2024). Understanding the diversity of HLA alleles and the immunodominance of specific EBV peptides, such as those from EBNA1 and LMP2, is critical for the development of effective, HLA-matched immunotherapies (BMJ, 2021).

Other names

Epstein–Barr virus peptide antigens presented by MHC class IEBV peptide-HLA class I complexEBV antigen-MHC class I complexEBV-specific MHC-I complexEBV pMHC

T-cell receptor (TCR) binding to the peptide-MHC complex, leading to the activation of cytotoxic T lymphocytes and subsequent lysis of EBV-infected cells via perforin and granzyme release.