Epstein-Barr virus BamHI-A rightward frame 1-derived peptide–Major Histocompatibility Complex (BARF1-pMHC)

BARF1-derived peptide–MHC complexes are specialized molecular targets formed when the Epstein-Barr virus (EBV) protein BARF1 is processed into short peptides and presented on the surface of infected cells by Major Histocompatibility Complex (MHC) molecules (Taylor et al., 2004, PubMed: 15140981). BARF1 itself is a secreted hexameric protein that functions as a decoy receptor for colony-stimulating factor 1 (CSF-1), thereby suppressing host macrophage activity and promoting immune evasion (Hoebe et al., 2012, PubMed: 22933282). In the context of EBV-associated malignancies such as nasopharyngeal carcinoma (NPC) and EBV-positive gastric cancer, BARF1 is consistently expressed, making its peptide-MHC complexes attractive targets for immunotherapy (Seto et al., 2005, PubMed: 15650188). Because these complexes are derived from a viral protein, they offer high tumor specificity with minimal risk of targeting healthy non-infected tissues. Current therapeutic development focuses on T-cell receptor (TCR) engineered T-cells and TCR-like antibodies that can specifically recognize the BARF1 peptide (e.g., VLPGLAVIS) in the groove of HLA molecules like HLA-A*02:01 (Lin et al., 2018, PubMed: 29752335). These interventions aim to trigger a potent cytotoxic immune response against EBV-transformed malignant cells while sparing normal host cells.

Other names

BARF1-HLA complexBARF1 peptide-MHC complexEBV BARF1-pMHCBARF1-HLA-A*02:01 complex

Recognition of the specific viral peptide presented by MHC molecules by engineered T-cell receptors (TCRs) or TCR-like antibodies, triggering cytotoxic T-lymphocyte (CTL) mediated lysis of the target cell.