Epstein-Barr virus BMLF1 peptide–HLA-A*02:01 complex (BMLF1-HLA-A2)

The BMLF1 peptide–MHC complex consists of an immunodominant peptide derived from the Epstein-Barr virus (EBV) BMLF1 protein (also known as SM or Mta), typically the GLCTLVAML sequence (residues 280–288), bound to a Major Histocompatibility Complex (MHC) class I molecule, most commonly HLA-A*02:01 (UniProt: P03202; IEDB: 17887). BMLF1 is an early lytic cycle protein of EBV that functions as an mRNA export factor, making it a critical marker for cells undergoing active viral replication (Steven et al., J Exp Med, 1997). This complex is a primary target for the host's cellular immune response, specifically recognized by CD8+ cytotoxic T lymphocytes (CTLs) via their T-cell receptors (TCRs) (Long et al., J Exp Med, 2005). In therapeutic contexts, this complex is targeted by TCR-engineered T-cell therapies and TCR-like antibodies to treat EBV-associated malignancies such as nasopharyngeal carcinoma and certain lymphomas (Sun et al., Front Immunol, 2022). It also serves as a key component in the development of therapeutic vaccines and diagnostic tools like MHC tetramers to monitor EBV-specific immune status. Effective targeting of this complex allows for the selective elimination of EBV-infected cells while sparing healthy tissue, although challenges include potential cross-reactivity with similar human peptides.

Other names

GLCTLVAML-HLA-A*02:01 complexEBV BMLF1(280-288) peptide-MHCBMLF1-MHC class I complexSM protein peptide-MHCMta peptide-MHC

The complex acts as a ligand for specific T-cell receptors (TCRs) on CD8+ cytotoxic T lymphocytes, triggering the release of perforins and granzymes to induce apoptosis in EBV-infected cells (Steven et al., J Exp Med, 1997).