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The Alpha-fetoprotein peptide–HLA-A2 complex consists of a short peptide (typically 9–10 amino acids) derived from the tumor-associated antigen alpha-fetoprotein (AFP) non-covalently bound to the antigen-presenting groove of the HLA-A2 molecule, a member of the MHC class I family. This complex is displayed on the surface of tumor cells (mainly hepatocellular carcinoma) and is recognized by cytotoxic T lymphocytes, allowing immune targeting of malignant cells. AFP-derived peptides, such as AFP(158-166) or AFP(325-334), are selected for their affinity to HLA-A2 and immunogenicity, forming a stable pMHC structure which is the basis for peptide vaccines and TCR-T therapies against HCC and other AFP-expressing cancers. This target is highly specific to immunotherapy research, as it enables the immune system to selectively eliminate cancer cells expressing fetal antigens re-expressed during oncogenesis.
Activation of cytotoxic T lymphocytes (CTLs) to recognize and kill AFP-expressing tumor cells Enhanced antigen presentation to prime T cell responses Vaccination strategies induce CTLs that specifically target tumor cells presenting this complex
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