Peptide–Human Leukocyte Antigen B*57:01 complex (pHLA-B*57:01)

The Peptide–HLA-B*57:01 complex is a specific Major Histocompatibility Complex (MHC) class I molecule bound to an antigenic peptide, typically derived from HIV-1 proteins like Gag (e.g., the KAFSPEVIPMF epitope), and displayed on the surface of infected CD4+ T cells [1][2]. This complex is a critical determinant of HIV-1 control; individuals carrying the HLA-B*57:01 allele are frequently 'elite controllers' who maintain low viral loads due to the high efficiency of CD8+ T cells in recognizing these specific pHLA complexes [1][3]. In drug development, this complex is targeted by novel immunotherapies such as Immune mobilizing monoclonal TCRs Against Virus (ImmTAVs) and TCR-like antibodies designed to eliminate the latent HIV reservoir [4]. Furthermore, HLA-B*57:01 is the primary mediator of abacavir hypersensitivity, where the drug binds to the F-pocket of the HLA molecule, altering its peptide-binding specificity and triggering a systemic inflammatory response [5][6]. Therapeutic strategies focusing on this target must navigate the high risk of hypersensitivity and ensure extreme specificity to avoid attacking non-infected cells presenting self-peptides [5].

Other names

HLA-B*57:01-peptide complexMHC class I-peptide complex (B*57:01)HIV-1 peptide-HLA-B*57:01Gag peptide-HLA-B*57:01 complex

Antigen recognition by CD8+ T-cell receptors; Drug-induced alteration of the peptide-binding groove (F-pocket) leading to neoantigen presentation; Redirection of T-cells via bispecific TCR molecules.