Epstein-Barr virus peptide-HLA class I complex (EBV pHLA-I) (EBV pHLA-I)

Epstein-Barr virus (EBV) peptides presented on HLA class I molecules are specific molecular complexes found on the surface of EBV-infected cells, including various types of cancer cells (Taylor et al., 2015). These complexes are formed when viral proteins, such as Latent Membrane Proteins (LMP1, LMP2) or EBV Nuclear Antigens (EBNA), are processed by the proteasome and loaded onto HLA class I molecules in the endoplasmic reticulum (Long et al., 2011). Once displayed on the cell surface, they act as targets for the immune system, specifically for CD8+ cytotoxic T cells. In the context of EBV-associated malignancies like nasopharyngeal carcinoma and post-transplant lymphoproliferative disorder, these complexes serve as highly specific neoantigens (Prockop et al., 2020). Therapeutic interventions, such as adoptive T-cell therapy (e.g., Tabelecleucel) and TCR-engineered cells, are designed to recognize these pHLA complexes to selectively eliminate tumor cells while sparing healthy, non-infected tissue (EMA, 2022). Because these antigens are of viral origin, they offer high specificity for tumor cells compared to healthy tissues, though HLA restriction and viral immune evasion mechanisms remain significant challenges. The interaction between the therapeutic T-cell receptor and the pHLA complex triggers a cytotoxic response that leads to the destruction of the malignant cell.

Other names

EBV pMHCEBV-specific HLA-restricted antigensEBV-derived epitopesEBV-derived peptides presented on HLA class I molecules on EBV-infected tumor cells

Therapeutic agents, such as EBV-specific T-cells or TCR-T cells, utilize T-cell receptors to specifically bind the EBV peptide-HLA complex on the tumor cell surface (Prockop et al., 2020). This binding triggers the formation of an immunological synapse, leading to the release of cytotoxic granules containing perforin and granzymes, which induce apoptosis in the target cell (Long et al., 2011).