TAPBPR promotes editing of the HLA-B44 peptide repertoire, increasing the presentation of peptides containing a C-terminal tryptophan.

ABSTRACT: Major histocompatibility complex class I (MHC-I) molecules play a key part in the adaptive immune response by presenting antigens to CD8⁺ T cells. The high degree of polymorphism in MHC-I leads to significant variation in their dependence on the components of the antigen processing and presentation pathway, such as the transporter associated with antigen processing (TAP) and tapasin, and their affinity for the peptide editor TAP-binding protein related (TAPBPR). Here, we investigated the influence of TAPBPR on the cell surface phenotype and peptide repertoire presented by two human leukocyte antigen (HLA) class I allotypes, HLA-B*44:02 and HLA-B*44:05, which are known to differ drastically in their dependence on tapasin. TAPBPR bound weakly to both HLA-B*44:02 and HLA-B*44:05. I

SUBMITTER: Aflalo A 

PROVIDER: S-EPMC12615179 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature