The glycosylation status of MHC class I molecules impacts their interactions with TAPBPR
| Autor: | Ilca, F Tudor, Boyle, Louise |
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| Přispěvatelé: | Boyle, Louise [0000-0002-3105-6555], Apollo - University of Cambridge Repository |
| Rok vydání: | 2021 |
| Předmět: |
Antigen processing and presentation
Antigen Presentation Glycosylation Histocompatibility Antigens Class I Immunoglobulins Membrane Proteins chemical and pharmacologic phenomena Peptide exchange Peptide editing carbohydrates (lipids) TAPBPR/TAPBPL Humans lipids (amino acids peptides and proteins) MHC HeLa Cells |
| Popis: | 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-A*68:02, -A*02:01 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. |
| Databáze: | OpenAIRE |
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