Alpha-fetoprotein peptide–major histocompatibility complex class I complex (AFP–MHC class I complex)

The **alpha-fetoprotein peptide–major histocompatibility complex class I complex** (AFP–MHC class I complex) consists of a peptide selectively derived from the **alpha-fetoprotein (AFP)** protein, which is presented on the cell surface by **MHC class I molecules (typically HLA-A alleles such as HLA-A*02:01)**[2][3]. This complex is a key target for immunotherapy against AFP-expressing tumors, most notably **hepatocellular carcinoma**. The AFP peptide is processed and loaded onto MHC class I in tumor cells, displayed on the surface, and recognized by cytotoxic T cells. Therapeutic strategies include vaccines to elicit T cell responses against AFP, and novel antibodies or bispecific constructs that specifically bind the AFP peptide/MHC class I complex on tumor cells, aiming to mediate tumor cell killing while sparing normal tissues. The presence of these complexes can serve as both a therapeutic target and a **biomarker** for selecting patients with AFP-expressing cancers. Safety and efficacy are subjects of ongoing clinical investigation due to concerns of immune tolerance and specificity[2][3][6].

Other names

AFP/MHC class I complexAFP peptide–HLA class I complexAFP–HLA complexAFP peptide–MHC complexAMC (in some literature)

Immune activation via presentation of AFP-derived epitopes to cytotoxic T lymphocytes (CTLs) through MHC class I, leading to targeted killing of AFP-expressing tumor cells. Antibody binding to cell-surface AFP peptide–MHC class I complex, enabling recruitment of immune effector mechanisms (e.g., antibody-dependent cell-mediated cytotoxicity). Vaccine-induced T cell priming through recognition of AFP-derived peptide/MHC complexes on antigen-presenting cells.