MART-1 peptide–HLA-A2 complex (None established in major databases; the epitope is sometimes referred to by sequence (e.g., MART-1_26–35/HLA-A2 or ELA/HLA-A2))

The MART-1 peptide–HLA-A2 complex is formed when a short epitope, most commonly spanning amino acids 26–35 or 27–35 of the MART-1 (Melan-A) protein, is presented in the peptide-binding groove of the human MHC class I molecule HLA-A2[6][4][1]. This complex is recognized by cytotoxic T lymphocytes (CD8+ T cells) via their T cell receptors, allowing the immune system to identify and destroy melanoma cells expressing MART-1[6][4][1]. The MART-1/HLA-A2 complex is a prevalent and immunodominant target in HLA-A2-positive melanoma patients and underpins multiple cancer vaccine and adoptive T cell therapy strategies. Structural studies reveal that the complex can adopt different conformations depending on peptide sequence, with implications for immune recognition and therapeutic design[1][5]. Challenges include natural variation in antigen processing/presentation and potential induction of autoimmunity against normal melanocytes[4][6].

Other names

Melan-A peptide/HLA-A2 complexMART-1/HLA-A2 complexMART-1 epitope/HLA-A2EAAGIGILTV–HLA-A2 complexMART-1_26–35/HLA-A2Melan-A_26–35/HLA-A2ELA/HLA-A2MART-1_27–35/HLA-A2

Induction of CD8+ T cell-mediated immune response via recognition by T cell receptors (TCRs) on effector lymphocytes Engineered TCR recognition leading to cytotoxicity against MART-1-expressing melanoma cells