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Human leukocyte antigen A*32:07 (HLA-A*32:07) is a specific allele of the HLA-A gene, which encodes a major histocompatibility complex (MHC) class I heavy chain (IPD-IMGT/HLA Database, 2024). This protein is expressed on the surface of almost all nucleated cells and plays a vital role in the adaptive immune system by presenting processed endogenous peptides to CD8+ cytotoxic T cells (UniProt, 2024). By displaying these peptides, HLA-A*32:07 allows the immune system to distinguish between self-antigens and non-self antigens, such as those from viruses or tumors (PubMed, PMID: 32814060). This specific allele is characterized by an Arg156Cys substitution in the alpha-2 domain, which forms part of the peptide-binding groove and likely influences the repertoire of presented peptides (PubMed, PMID: 12100496). In the field of pharmacogenomics, HLA-A*32 alleles are significant biomarkers for predicting severe cutaneous adverse reactions (SCARs), most notably Vancomycin-induced Drug Reaction with Eosinophilia and Systemic Symptoms (DRESS) (StatPearls, 2023). The interaction between drugs and the HLA-A*32:07 molecule can trigger an inappropriate T-cell response through mechanisms such as the p-i model or the hapten/pro-hapten model (Pharmacogenomics Journal, 2021). Consequently, HLA-A*32:07 is a target for genetic screening to improve drug safety and is also relevant in the context of transplant immunology and HLA-restricted immunotherapy (NIH, 2024).
Presentation of drug-modified peptides or direct pharmacological interaction with the HLA-peptide-TCR complex (p-i mechanism) to trigger an immune response (PubMed, PMID: 32814060).
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