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The glycosylation status of MHC class I molecules impacts their interactions with TAPBPR

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Ilca, F Tudor 


Glycosylation plays a crucial role in the folding, structure, quality control and trafficking of glycoproteins. Here, we explored whether the glycosylation status of MHC class I (MHC-I) molecules impacts their affinity for the peptide editor, TAPBPR. We demonstrate that the interaction between TAPBPR and MHC-I is stronger when MHC-I lacks a glycan. Subsequently, TAPBPR can dissociate peptides, even those of high affinity, more easily from non-glycosylated MHC-I compared to their glycosylated counterparts. In addition, TAPBPR is more resistant to peptide-mediated allosteric release from non-glycosylated MHC-I compared to species with a glycan attached. Consequently, we find the glycosylation status of HLA-A68:02, -A02:01 and –B*27:05 influences their ability to undergo TAPBPR-mediated peptide exchange. The discovery that the glycan attached to MHC-I significantly influences the affinity of their interactions with TAPBPR has important implications, on both an experimental level and in a biological context.



Antigen processing and presentation, Glycosylation, MHC, Peptide editing, Peptide exchange, TAPBPR/TAPBPL, Antigen Presentation, Glycosylation, HeLa Cells, Histocompatibility Antigens Class I, Humans, Immunoglobulins, Membrane Proteins

Journal Title

Molecular Immunology

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Wellcome Trust (219479/Z/19/Z)
Wellcome Trust (109076/Z/15/Z)