ArticleScience advances2023
Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Reconstitution of glycan-driven MHC-I recycling reveals calreticulin as mediator between TAPBPR and tapasin.The EMBO journal · 2026Article
- Engineering high-fidelity tapasin variants to enhance MHC-I antigen presentation.The Journal of biological chemistry · 2026Article
- Mouse TAPBPR shows functional similarity to human TAPBPR in shaping the MHC-I immunopeptidome.Frontiers in immunology · 2026Article
- High-Throughput Production of Class I MHC Tetramers for Immunological Studies Using Chaperone-Mediated Peptide Exchange.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Targeting peptide antigens using a multiallelic MHC I-binding system.Nature biotechnology · 2025Article
- 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
- Evidence of focusing the MHC class I immunopeptidome by tapasin.Frontiers in immunology · 2025Article
- How conformational changes near the F pocket of MHC class I proteins mediate chaperone assisted peptide loading.Frontiers in immunology · 2025Article
- Review
- Conformational plasticity of RAS Q61 family of neoepitopes results in distinct features for targeted recognition.Nature communications · 2023Article
- Structural principles of peptide-centric chimeric antigen receptor recognition guide therapeutic expansion.Science immunology · 2023Article
- A Chicken Tapasin ortholog can chaperone empty HLA-B∗37:01 molecules independent of other peptide-loading components.The Journal of biological chemistry · 2023Article
- Article
- 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
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Immunological chaperones tapasin and TAP binding protein, related (TAPBPR) play key roles in antigenic peptide optimization and quality control of nascent class I major histocompatibility complex (MHC-I) molecules. The polymorphic nature of MHC-I proteins leads to a range of allelic dependencies on chaperones for assembly and cell-surface expression, limiting chaperone-mediated peptide exchange to a restricted set of human leukocyte antigen (HLA) allotypes. Here, we demonstrate and characterize xeno interactions between a chicken TAPBPR ortholog and a complementary repertoire of HLA allotypes, relative to its human counterpart. We find that TAPBPR orthologs recognize empty MHC-I with broader allele specificity and facilitate peptide exchange by maintaining a reservoir of receptive molecules. Deep mutational scanning of human TAPBPR further identifies gain-of-function mutants, resembling the chicken sequence, which can enhance HLA-A*01:01 expression in situ and promote peptide exchange in vitro. These results highlight that polymorphic sites on MHC-I and chaperone surfaces can be engineered to manipulate their interactions, enabling chaperone-mediated peptide exchange on disease-relevant HLA alleles.
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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.