HLA class I histocompatibility antigen, B-41 alpha chain (HLA-B*41)

HLA-B*41 (HLA class I histocompatibility antigen, B-41 alpha chain) is a member of the major histocompatibility complex (MHC) class I family, functioning as a highly polymorphic cell-surface glycoprotein. Its primary biological role is to bind and present endogenous peptide fragments, derived from intracellular proteins, viruses, or tumor antigens, to CD8+ cytotoxic T cells to initiate an adaptive immune response. HLA-B*41 is clinically significant as a biomarker for various immune-mediated conditions; specifically, the HLA-B*41:02 allele is associated with susceptibility to Henoch-Schönlein purpura (IgA vasculitis), and HLA-B*41:01 has been linked to hypersensitivity reactions against beta-lactam antibiotics like amoxicillin. In oncology, HLA-B*41 serves as a potential target for HLA-restricted immunotherapies and personalized cancer vaccines, although tumors often downregulate its expression to achieve immune escape. Pharmacological interactions can occur through the p-i (pharmacological interaction with immune receptors) mechanism or the altered peptide repertoire model, leading to adverse drug reactions.

Other names

MHC class I antigen B*41Major histocompatibility complex, class I, BHLA-B41HLA-B*41:01HLA-B*41:02Human leukocyte antigen B

Presentation of peptide fragments to CD8+ T cells; non-covalent drug binding (p-i mechanism); alteration of the peptide-binding repertoire