ArticleProceedings of the National Academy of Sciences of the United States of America2018
Utilizing TAPBPR to promote exogenous peptide loading onto cell surface MHC I molecules.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The trial behind it
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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- Engineering high-fidelity tapasin variants to enhance MHC-I antigen presentation.The Journal of biological chemistry · 2026Article
- Utilizing TAPBPR for Peptide Loading, Dissociation, and Exchange on Plasma Membrane-Expressed MHC-I.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Identification of novel HLA class I-restricted hepatitis B virus peptides and their modulation by peptide editor TAPBPR.Frontiers in immunology · 2026Article
- Mouse TAPBPR shows functional similarity to human TAPBPR in shaping the MHC-I immunopeptidome.Frontiers in immunology · 2026Article
- Molecular Insights Into MR1-Mediated T Cell Immunity: Lessons Learned and Unanswered Questions.Immunological reviews · 2025Review
- CryoEM structure of an MHC-I/TAPBPR peptide-bound intermediate reveals the mechanism of antigen proofreading.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The potential applications of peptide-loading complex in cancer treatment.Frontiers in immunology · 2025Review
- TAPBPR promotes editing of the HLA-B44 peptide repertoire, increasing the presentation of peptides containing a C-terminal tryptophan.Frontiers in immunology · 2025Article
- Exercise-Dependent Modulation of Immunological Response Pathways in Endurance Athletes With and Without Atrial Fibrillation.Journal of the American Heart Association · 2024Article
- Reanalysis of Immunopeptidomics Datasets Provides Mechanistic Insight into TAPBPR-Mediated Peptide Editing on HLA-A, -B and -C Molecules.Wellcome open research · 2024Article
- A Chicken Tapasin ortholog can chaperone empty HLA-B∗37:01 molecules independent of other peptide-loading components.The Journal of biological chemistry · 2023Article
- EULAR study group on 'MHC-I-opathy': identifying disease-overarching mechanisms across disciplines and borders.Annals of the rheumatic diseases · 2023Review
- Universal open MHC-I molecules for rapid peptide loading and enhanced complex stability across HLA allotypes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes.Science advances · 2023Article
- Chaperone function in antigen presentation by MHC class I molecules-tapasin in the PLC and TAPBPR beyond.Frontiers in immunology · 2023Review
- TAPBPR employs a ligand-independent docking mechanism to chaperone MR1 molecules.Nature chemical biology · 2022Article
- Therapeutic Strategies to Enhance Tumor Antigenicity: Making the Tumor Detectable by the Immune System.Biomedicines · 2022Review
- Targeting the antigen processing and presentation pathway to overcome resistance to immune checkpoint therapy.Frontiers in immunology · 2022Review
- The glycosylation status of MHC class I molecules impacts their interactions with TAPBPR.Molecular immunology · 2021Article
- The Role of Antigen Processing and Presentation in Cancer and the Efficacy of Immune Checkpoint Inhibitor Immunotherapy.Cancers · 2021Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The repertoire of peptides displayed at the cell surface by MHC I molecules is shaped by two intracellular peptide editors, tapasin and TAPBPR. While cell-free assays have proven extremely useful in identifying the function of both of these proteins, here we explored whether a more physiological system could be developed to assess TAPBPR-mediated peptide editing on MHC I. We reveal that membrane-associated TAPBPR targeted to the plasma membrane retains its ability to function as a peptide editor and efficiently catalyzes peptide exchange on surface-expressed MHC I molecules. Additionally, we show that soluble TAPBPR, consisting of the luminal domain alone, added to intact cells, also functions as an effective peptide editor on surface MHC I molecules. Thus, we have established two systems in which TAPBPR-mediated peptide exchange on MHC class I can be interrogated. Furthermore, we could use both plasma membrane-targeted and exogenous soluble TAPBPR to display immunogenic peptides on surface MHC I molecules and consequently induce T cell receptor engagement, IFN-γ secretion, and T cell-mediated killing of target cells. Thus, we have developed an efficient way to by-pass the natural antigen presentation pathway of cells and load immunogenic peptides of choice onto cells. Our findings highlight a potential therapeutic use for TAPBPR in increasing the immunogenicity of tumors in the future.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.