Epstein-Barr virus-derived peptide antigens presented on Major Histocompatibility Complex molecules (EBV-pMHC)

Epstein-Barr virus (EBV)-derived peptide antigens presented on Major Histocompatibility Complex (MHC) molecules, also known as Human Leukocyte Antigen (HLA) molecules in humans, represent the molecular interface through which the immune system identifies EBV-infected cells (Taylor et al., 2015, PMID: 25617115). These targets consist of short viral peptides, typically 8-11 amino acids for MHC Class I, derived from latent or lytic viral proteins such as EBNA1, LMP1, and LMP2, which are nested within the peptide-binding groove of the MHC molecule (Long et al., 2011, PMID: 21149605). This presentation is essential for the activation and effector function of EBV-specific cytotoxic T-lymphocytes (CTLs), which recognize the complex via their T-cell receptors (TCRs). In clinical practice, these complexes are the focus of adoptive immunotherapies, such as tabelecleucel (Ebvallo), which utilizes allogeneic EBV-specific T-cells to treat EBV-positive post-transplant lymphoproliferative disorder (EMA, 2022). Furthermore, these antigens are implicated in the pathogenesis of EBV-associated malignancies and autoimmune conditions like multiple sclerosis, where molecular mimicry between EBV peptides and self-antigens is a hypothesized mechanism (Bjornevik et al., 2022, PMID: 35025605). Therapeutic strategies targeting these pMHC complexes include TCR-engineered T-cells and peptide-based vaccines designed to bolster the endogenous immune response against the virus.

Other names

EBV-pHLAEpstein-Barr virus peptide-HLA complexesEBV-specific antigensEBV-pMHC complexesEBV-restricted antigens

Recognition by T-cell receptors (TCRs) on cytotoxic T-lymphocytes (CTLs) leading to targeted lysis of EBV-infected cells and cytokine production.