Epstein-Barr virus peptide–HLA complex on infected B cell (EBV peptide–HLA complex)

The Epstein-Barr virus peptide–HLA complex on infected B cells is a molecular complex formed when short polypeptide fragments (epitopes) derived from EBV proteins are loaded onto human leukocyte antigen (HLA) molecules on the surface of B cells infected with EBV[2][3][5]. Class I HLA molecules present EBV peptides to CD8+ cytotoxic T cells, mediating immune surveillance and cytolytic clearance of infected cells, while class II HLA molecules present antigens to CD4+ T helper cells and are also a critical attachment receptor for EBV entry via gp42[2][3][4]. This complex is a focus of immunotherapeutic and vaccine strategies due to its specificity for EBV infection and its visibility to adaptive immune cells[5][9][7]. Altered EBV peptide–HLA presentation can affect susceptibility to EBV-driven malignancies, immune evasion, and antiviral immune responses[3][7]. If further molecular specificity is required (e.g., which peptide and which HLA allele), a precise name should be assigned, such as “Epstein-Barr virus EBNA3A peptide (FLRGRAYGL)–HLA-A*02:01 complex.”

Other names

EBV epitope–HLA complexEpstein-Barr virus peptide–MHC complexEBV antigen–presenting complexEBV–HLA class I complexEBV–HLA class II complex

Immune recognition: TCRs on cytotoxic T lymphocytes (CTLs) recognize these complexes, leading to targeted killing of infected B cells[5][9][7]. Antibody-dependent cellular cytotoxicity (ADCC): TCR-mimic antibodies bind the peptide–HLA complex, flagging cells for immune elimination[3]. NK cell activation/inhibition: EBV peptides bound to HLA-E can modulate NK cell inhibition[7].