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.
journal_name
Elifejournal_title
eLifeauthors
Hermann C,van Hateren A,Trautwein N,Neerincx A,Duriez PJ,Stevanović S,Trowsdale J,Deane JE,Elliott T,Boyle LHdoi
10.7554/eLife.09617subject
Has Abstractpub_date
2015-10-06 00:00:00issn
2050-084Xjournal_volume
4pub_type
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