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The PR1/HLA-A2 complex is a peptide-MHC class I molecule, where the PR1 peptide (VLQELNVTV, a nonamer) derived from proteinase 3 and neutrophil elastase is presented on the cell surface by the HLA-A*02:01 molecule. This complex is specifically recognized by cytotoxic T lymphocytes and monoclonal antibodies, making it a well-studied target for immunotherapy in acute/chronic myeloid leukemia. It is not a traditional receptor or enzyme, but an immune complex critical to adaptive immune recognition and a central neoantigen in targeted cancer therapy. The PR1 peptide is processed and presented by leukemic (and some normal myeloid) cells, enabling immune targeting in HLA-A2–positive patients. PR1/HLA-A2 surface abundance serves as a biomarker and basis for approaches including TCR-based therapies and antibody immunotherapy.
Immune-mediated cytotoxicity via T cells recognizing PR1/HLA-A2 on leukemic cells; Antibody-dependent cellular cytotoxicity (e.g., by 8F4 mAb); Complement-dependent cytotoxicity.
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