Epstein-Barr virus latent membrane protein 2 peptide–major histocompatibility complex class I (LMP2-pMHC)

The Epstein-Barr virus (EBV) latent membrane protein 2 (LMP2) peptide–major histocompatibility complex class I (MHC-I) is a molecular assembly presented on the surface of cells infected with EBV (UniProt: P13285). LMP2 is a transmembrane protein essential for maintaining viral latency and is frequently expressed in EBV-associated malignancies such as nasopharyngeal carcinoma and certain lymphomas (PubMed: 25239444). Within the cell, LMP2 is proteolytically processed into short antigenic peptides, which are then transported to the endoplasmic reticulum and loaded onto MHC-I molecules. The resulting pMHC complex is displayed on the cell surface, where it acts as a specific ligand for the T-cell receptors (TCRs) of CD8+ cytotoxic T cells (PubMed: 30104343). This interaction is a cornerstone of the adaptive immune response against EBV-positive tumors, making the complex a primary target for adoptive T-cell therapies and vaccines. Therapeutic strategies often focus on specific immunodominant epitopes, such as the HLA-A*02:01-restricted peptide CLGGLLTMV. Drugs targeting this complex, including engineered TCR-T cells and virus-specific lymphocytes like Tabelecleucel, aim to induce apoptosis in tumor cells by mimicking or enhancing natural immune recognition (EMA: Ebvallo). However, the efficacy of these treatments can be hindered by tumor-mediated HLA downregulation or the development of immune exhaustion within the tumor microenvironment.

Other names

EBV LMP2-MHC complexLMP2 peptide-HLA complexHLA-A2/LMP2 complexLMP2-pMHCLatent membrane protein 2-derived peptide–MHC-I complex

Recognition by T-cell receptors (TCRs) on CD8+ cytotoxic T cells, leading to targeted lysis of EBV-infected or transformed cells.