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Breast cancer anti-estrogen resistance protein 3 phosphopeptide epitope (pBCAR3 126-134) is a specific cancer-associated neoantigen derived from the BCAR3 adapter protein. BCAR3 is a member of the NSP family that regulates cell signaling pathways involved in breast cancer resistance to anti-estrogen therapies and promotes cell migration and invasion (UniProt O75815). The pBCAR3 epitope consists of a nine-amino acid sequence (residues 126-134) that is phosphorylated at Threonine 130 and presented on the cell surface by the HLA-A*0201 major histocompatibility complex (MHC) class I molecule. This phosphorylation-dependent epitope is highly specific to malignant cells, such as those in melanoma and breast cancer, while being largely absent in normal tissues (Journal for ImmunoTherapy of Cancer, 2020). Consequently, it serves as a promising target for cancer immunotherapy, particularly for the development of peptide-based vaccines designed to stimulate a CD8+ T-cell response. Clinical trials have evaluated the safety and immunogenicity of vaccines targeting this epitope, often in combination with other phospho-neoantigens like pIRS2. By priming the immune system to recognize this specific post-translational modification, these therapies aim to provide a highly selective mechanism for tumor cell destruction.
Induction of a specific CD8+ T-cell immune response against tumor cells presenting the phosphorylated BCAR3 peptide in the context of HLA-A*0201.
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