TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst.
Published version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
Abstract
Our understanding of the antigen presentation pathway has recently been enhanced with the identification that the tapasin-related protein TAPBPR is a second major histocompatibility complex (MHC) class I-specific chaperone. We sought to determine whether, like tapasin, TAPBPR can also influence MHC class I peptide selection by functioning as a peptide exchange catalyst. We show that TAPBPR can catalyse the dissociation of peptides from peptide-MHC I complexes, enhance the loading of peptide-receptive MHC I molecules, and discriminate between peptides based on affinity in vitro. In cells, the depletion of TAPBPR increased the diversity of peptides presented on MHC I molecules, suggesting that TAPBPR is involved in restricting peptide presentation. Our results suggest TAPBPR binds to MHC I in a peptide-receptive state and, like tapasin, works to enhance peptide optimisation. It is now clear there are two MHC class I specific peptide editors, tapasin and TAPBPR, intimately involved in controlling peptide presentation to the immune system.
Description
Keywords
Journal Title
Conference Name
Journal ISSN
2050-084X
Volume Title
Publisher
Publisher DOI
Sponsorship
Royal Society (1562)
The Royal Society (uf100371)
Wellcome Trust (104647/Z/14/Z)
Wellcome Trust (100140/Z/12/Z)
Wellcome Trust (089821/Z/09/Z)
Wellcome Trust (089563/Z/09/Z)