Abstract：
:Understanding how peptide selection is controlled on different major histocompatibility complex class I (MHC I) molecules is pivotal for determining how variations in these proteins influence our predisposition to infectious diseases, cancer, and autoinflammatory conditions. Although the intracellular chaperone TAPBPR edits MHC I peptides, it is unclear which allotypes are subjected to TAPBPR-mediated peptide editing. Here, we examine the ability of 97 different human leukocyte antigen (HLA) class I allotypes to interact with TAPBPR. We reveal a striking preference of TAPBPR for HLA-A, particularly for supertypes A2 and A24, over HLA-B and -C molecules. We demonstrate that the increased propensity of these HLA-A molecules to undergo TAPBPR-mediated peptide editing is determined by molecular features of the HLA-A F pocket, specifically residues H114 and Y116. This work reveals that specific polymorphisms in MHC I strongly influence their susceptibility to chaperone-mediated peptide editing, which may play a significant role in disease predisposition.
journal_name
Cell Repjournal_title
Cell reportsauthors
Ilca FT,Drexhage LZ,Brewin G,Peacock S,Boyle LHdoi
10.1016/j.celrep.2019.09.074subject
Has Abstractpub_date
2019-11-05 00:00:00pages
1621-1632.e3issue
6issn
2211-1247pii
S2211-1247(19)31271-9journal_volume
29pub_type
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