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

Epstein-Barr virus (EBV) antigens presented as peptide–major histocompatibility complexes (pMHC) are specialized molecular targets found on the surface of cells infected with EBV, particularly in the context of EBV-associated malignancies (Taylor et al., 2015). These complexes are formed when viral proteins, such as Epstein-Barr nuclear antigen 1 (EBNA1) or latent membrane proteins (LMP1 and LMP2), are proteolytically processed into short peptides and loaded onto MHC Class I or II molecules (Long et al., 2011). In cancers like nasopharyngeal carcinoma, Hodgkin lymphoma, and post-transplant lymphoproliferative disorder (PTLD), these pMHC complexes serve as highly specific markers that distinguish malignant cells from healthy, non-infected tissue (Prockop et al., 2020). Therapeutic strategies targeting these complexes include adoptive T-cell therapies, such as tabelecleucel, and engineered T-cell receptor (TCR) therapies that recognize the viral peptide in the context of a specific HLA allele (Haque et al., 2007). The interaction between the therapeutic T-cell and the pMHC complex induces a targeted cytotoxic response, leading to the destruction of the tumor cell. However, the clinical utility of these therapies is often constrained by the requirement for HLA matching and the potential for tumors to escape immune detection by downregulating MHC expression (Thorley-Lawson, 2001).

Other names

EBV-derived peptide–HLA complexEBV-specific pMHCEBV-associated tumor antigenEpstein-Barr virus peptide-MHCEBV pMHC complex

T-cell receptor (TCR) binding to the peptide-MHC complex, triggering T-cell activation and subsequent lysis of the target tumor cell (Prockop et al., 2020).