Epstein-Barr virus-derived peptide-major histocompatibility complex (EBV pMHC)

Epstein-Barr virus (EBV)-derived peptide antigens presented by major histocompatibility complex (MHC) molecules are specific molecular targets found on the surface of EBV-infected tumor cells. These targets consist of short viral peptide fragments, typically derived from latent proteins such as LMP1, LMP2, or EBNA1, which are loaded onto MHC Class I or II molecules (Taylor et al., 2015). In EBV-associated malignancies like nasopharyngeal carcinoma and post-transplant lymphoproliferative disorder (PTLD), these pMHC complexes serve as the primary recognition site for the host's cellular immune response. Therapeutic interventions, such as the approved T-cell therapy tabelecleucel, utilize T-cells with receptors specifically tuned to these viral pMHC complexes to selectively eliminate malignant cells (EMA, 2022). The clinical utility of these targets is highly dependent on the patient's HLA genotype, as specific MHC alleles are required to present particular EBV peptides effectively. Challenges in targeting these complexes include potential immune escape through the downregulation of MHC expression by the tumor and the risk of off-target toxicity if the viral peptide mimics a self-antigen.

Other names

EBV-specific peptide-HLA complexEBV-derived tumor antigensEBV-MHC complexEBV-associated peptide-MHCEpstein-Barr virus peptide-MHC

Recognition by T-cell receptors (TCRs) on cytotoxic T-lymphocytes, leading to the release of perforin and granzymes and subsequent apoptosis of the EBV-positive target cell (Janeway et al., 2001).