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BCR-ABL-derived peptides are short sequences of amino acids that span the unique fusion junction of the BCR-ABL protein, which results from the Philadelphia chromosome translocation (t(9;22)) (Bocchia et al., 2005). This fusion protein is the hallmark of chronic myeloid leukemia (CML) and some cases of acute lymphoblastic leukemia (ALL) (Maslak et al., 2008). Because the amino acid sequence at the fusion point is entirely neo-antigenic and not present in the normal human proteome, these peptides are ideal targets for immunotherapy (Rojas et al., 2007). They are typically utilized in the development of cancer vaccines or T-cell receptor (TCR) therapies designed to prime the patient's immune system to recognize and destroy leukemic cells (Cai et al., 2012). While tyrosine kinase inhibitors (TKIs) are the standard of care for inhibiting the BCR-ABL enzyme, peptide-based approaches are investigated to eradicate minimal residual disease and leukemic stem cells that TKIs may fail to eliminate (Scheinberg et al., 2003).
Stimulation of specific T-cell immunity by acting as an epitope presented by MHC molecules to induce a cytotoxic T-lymphocyte (CTL) response against leukemic cells.
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