Preferentially expressed antigen in melanoma peptide-major histocompatibility complex (PRAME peptide-MHC complex)

The PRAME peptide-MHC complex is formed when peptides derived from the intracellular PRAME protein, a cancer/testis antigen, are processed by the proteasome and loaded onto MHC molecules (typically class I such as HLA-A*02:01) for presentation on the surface of tumor cells[2][4]. This complex allows for specific recognition by CD8+ cytotoxic T lymphocytes or by engineered antibodies and T cells in immunotherapy applications[4][7]. Because PRAME itself is not present on the cell surface, but rather its presented peptides in complex with MHC, therapeutics targeting this complex offer a way to selectively attack PRAME-expressing cancer cells with minimal effect on healthy tissue[2][4][7]. To summarize, the "Preferentially expressed antigen in melanoma peptide-MHC complex" is a well-validated immunotherapeutic target for PRAME-positive cancers, recognized by both natural and engineered immune effectors, and is the focus of significant drug and biomarker development.

Other names

PRAME peptide-HLA complexPRAME/MHC complexPRAME/HLA-A*02:01 complex (specific for peptides such as ALYVDSLFFL bound to HLA-A2)PRAME antigen-MHC complex

T cell-mediated cytotoxicity: Recognition of tumor cells by T cells via the PRAME peptide-MHC complex Antibody-dependent cellular cytotoxicity (via TCRm antibodies that bind the complex)