Major histocompatibility complex class I–mammaglobin-A peptide complex (MHC-I–mammaglobin-A complex)

The Major histocompatibility complex class I–mammaglobin-A peptide complex is a molecular complex formed by the binding of a short peptide sequence derived from the mammaglobin-A protein within the groove of an MHC class I molecule (such as an HLA-A*02:01 allele)[1][4][8]. This complex is transported to the cell surface where it is recognized by cytotoxic T cells via their T cell receptor (TCR)[8][1]. The complex plays a fundamental role in immune surveillance by allowing T cells to distinguish mammaglobin-A–expressing tumor cells from normal tissue. It is a clinically relevant target for immunotherapies, especially against cancers with overexpression of mammaglobin-A, as it can be targeted by engineered T cells or TCR-mimic antibodies[7][8]. The specificity comes from both the MHC allele and the precise mammaglobin-A peptide presented, making this a highly selective, disease-relevant immune target.

Other names

pMHC-I–mammaglobin-AHLA–mammaglobin-A complexMammaglobin-A epitope–MHC-I complex(No widely-used single-word or gene-style aliases)

Targeted immune cell activation — Engineered TCRs or antibodies bind the mammaglobin-A–MHC-I complex, triggering cytotoxic T cell activity against cells presenting the complex[7][8]. Immune recognition modulation — Vaccination strategies lead to increased presentation and immune targeting of mammaglobin-A positive tumor cells.