The tapasin-related protein (TAPBPR) binds MHC class I molecules (MHC I) with high affinity and functions in a similar fashion to tapasin in vitro, suggesting TAPBPR is an additional MHC I peptide editor.

Van Hateren, Andrew (2014) The tapasin-related protein (TAPBPR) binds MHC class I molecules (MHC I) with high affinity and functions in a similar fashion to tapasin in vitro, suggesting TAPBPR is an additional MHC I peptide editor. 8th International Workshop on Antigen Processing and Presentation, The Academy of Natural Sciences of Drexel University, Philidelphia, United States. 10 - 13 Jun 2014.

Abstract

We investigated the hypothesis that TAPBPR provides an additional layer of quality control by analysing whether TAPBPR influences MHC I peptide selection in vitro.

We found TAPBPR :
binds MHC I with much higher affinity than tapasin;
enhances the ability of empty MHC I molecules to bind peptide;
catalyses dissociation of peptides from peptide-MHC I complexes;
edits the MHC I peptide repertoire via peptide exchange;
can function with at least one HLA–B allotype, in addition to the two HLA-A allotypes that have been studied to date.

Cumulatively our findings support the possibility that TAPBPR provides an additional quality control layer for at least some MHC I molecules.

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Contributors

Author: Andrew Van Hateren

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