ArticleMolecular immunology2021
The glycosylation status of MHC class I molecules impacts their interactions with TAPBPR.
Article in Molecular immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- L-Fucose: a dietary sugar with multifaceted potential in the biology and therapy of cancer.Nature reviews. Cancer · 2026Review
- Extensive Characterization of N-Glycosylation from Major Histocompatibility Complex with Hydrophilic Interaction Chromatography and Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Immunoproteomics: The Evolution from Classical Methods to Emerging Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Characterization of Human Leukocyte Antigen (HLA) Proteins with Integrated Immunopeptidomics and Proteomics Approach.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Decoding glycosylation potential from protein structure across human glycoproteins with a multi-view recurrent neural network.bioRxiv : the preprint server for biology · 2024Article
- Revisiting the immunopathology of congenital disorders of glycosylation: an updated review.Frontiers in immunology · 2024Review
- Conformational plasticity of RAS Q61 family of neoepitopes results in distinct features for targeted recognition.Nature communications · 2023Article
- Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes.Science advances · 2023Article
- High-Throughput, Quantitative Analysis of Peptide-Exchanged MHCI Complexes by Native Mass Spectrometry.Analytical chemistry · 2022Article
- GH18 family glycoside hydrolase Chitinase A of Salmonella enhances virulence by facilitating invasion and modulating host immune responses.PLoS pathogens · 2022Article
- Chaperones and Catalysts: How Antigen Presentation Pathways Cope With Biological Necessity.Frontiers in immunology · 2022Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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