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

Epstein–Barr virus-derived peptide–major histocompatibility complex (MHC) complexes are molecular assemblies formed when short peptides derived from EBV proteins are bound and presented by host cell MHC class I (and occasionally class II) molecules on the surface of infected or transformed cells. These complexes are recognized by CD8 T cells via their T cell receptor (TCR) as part of the adaptive immune surveillance against EBV infection. The specific peptide–MHC complexes can elicit potent cytotoxic responses, enabling the immune system to identify and destroy EBV-infected cells. However, EBV has evolved multiple mechanisms to interfere with the formation and presentation of these complexes, including viral proteins that inhibit antigen processing, reduce MHC expression, or directly interfere with peptide loading. In addition to their role in T cell activation, certain EBV peptides presented by non-classical MHC molecules such as HLA-E can modulate NK cell activity, either inhibiting or permitting NK cell-mediated cytotoxicity depending on the peptide sequence. EBV-derived peptide–MHC complexes represent important therapeutic and biomarker targets for immunotherapies (such as TCR-mimic antibodies and adoptive T cell transfer) and for the diagnosis and monitoring of EBV-associated diseases.

Other names

EBV peptide-MHC complexEpstein–Barr virus (EBV) peptide–MHC complexEBV pMHC complex

Induction of CD8 T cell-mediated cytotoxicity by recognition of viral peptide presented on MHC class I Modulation of NK cell responses via HLA-E-restricted EBV peptides Antibody-dependent cellular cytotoxicity mediated by antibodies specific for peptide–MHC complexes