Nov 5, 2018

TAPBPR mediates peptide dissociation from MHC class I using a leucine lever

BioRxiv : the Preprint Server for Biology
F Tudor IlcaLouise H Boyle


Tapasin and TAPBPR are known to perform peptide editing on major histocompatibility complex class I (MHC I) molecules, however, the precise molecular mechanism(s) involved in this process remain largely enigmatic. Here, using immunopeptidomics in combination with novel cell-based assays that assess TAPBPR-mediate peptide exchange, we reveal a critical role for the K22-D35 loop of TAPBPR in mediating peptide exchange on MHC I. We identify a specific leucine within this loop that enables TAPBPR to facilitate peptide dissociation from MHC I. Moreover, we delineate the molecular features of the MHC I F pocket required for TAPBPR to promote peptide dissociation in a loop-dependent manner. These data reveal that chaperone-mediated peptide editing of MHC I can occur by different mechanisms dependent on the C-terminal residue that the MHC I accommodates in its F pocket and provide novel insights that may inform the therapeutic potential of TAPBPR manipulation to increase tumour immunogenicity.

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Mentioned in this Paper

Carboxy-Terminal Amino Acid
Class 1
Major Histocompatibility Complex
Genes, MHC Class I
Molecular Chaperones
Terminal (End Postition)
Major histocompatibility complex protein
TAPBP gene

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