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The LMP2 peptide–MHC class I complex consists of a peptide derived from the Epstein-Barr virus (EBV) latent membrane protein 2 (LMP2), or less commonly from self-proteins, bound within the peptide-binding groove of a major histocompatibility complex class I molecule (such as HLA-A*11:01), which also associates with β2-microglobulin[3]. This complex is presented on the surface of infected or malignant cells and recognized by the T cell receptor on cytotoxic CD8+ T cells, triggering an immune response against EBV-infected or abnormal cells[3][5][6]. The generation of the LMP2 peptide is dependent on proteasomal degradation in the cytosol, which is often facilitated by immunoproteasome subunits such as LMP2 itself. Some LMP2 epitopes can be presented independently of the transporter associated with antigen processing (TAP), especially those with hydrophobic residues[6]. Presentation of this complex is central to adaptive immunity against EBV and has implications for immunotherapy in EBV-associated malignancies[3][6][7].
Drugs or therapies targeting this complex typically aim to stimulate cytotoxic T cell responses against infected or malignant cells presenting LMP2 peptides on MHC class I
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