Epstein-Barr virus peptide-major histocompatibility complex on infected cell

The **Epstein-Barr virus peptide-major histocompatibility complex (EBV peptide-MHC) on infected cells** refers to the complex formed when peptide fragments derived from EBV proteins are processed and presented by class I or class II human leukocyte antigen (HLA) molecules (the human form of major histocompatibility complex) on the surface of infected cells[1][4]. These complexes are essential for immune surveillance: they are recognized by T cell receptors on cytotoxic T lymphocytes, leading to targeted killing of EBV-infected cells[2][4][5]. Various EBV proteins yield immunodominant peptides (e.g., the Rta epitope, YVL-BR from BMLF1) that are presented by specific HLA alleles such as HLA-A*11:01 or HLA-A*02:01[1][5]. Some EBV-derived peptides can also bind to non-classical MHC molecules such as HLA-E, modulating NK cell activity[3]. EBV deploys several strategies to evade immune detection by interfering with the peptide-MHC pathway, such as downregulating MHC expression or blocking antigen processing[4]. Although no conventional drugs target the complex per se, it is a focus of immunotherapies, including TCR-mimic antibodies and adoptive T cell therapies, as a means to selectively eradicate EBV-infected or EBV-associated cancer cells[4][5].

Other names

EBV peptide–MHC complexEBV peptide–major histocompatibility complexEBV pMHCEpstein-Barr virus epitope-MHC complex

Immune recognition: Drugs and therapies aim to restore or enhance T cell or NK cell recognition of EBV peptide-MHC complexes by supplementing antigen presentation or redirecting immune specificity toward EBV epitopes[4].