ArticleThe Journal of experimental medicine2012
Structural insight into MR1-mediated recognition of the mucosal associated invariant T cell receptor.
Article in The Journal of experimental medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers, 1 of them a synthesis that pooled it.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
124 citing papers in PubMed, 1 synthesis or guideline pooled it, 188 citations in OpenAlex.
- Identification of a common variant with potential pleiotropic effect on risk of inflammatory bowel disease and colorectal cancer.Carcinogenesis · 2015Pooled it
- Hyper-Expression of PD-1 Is Associated with the Levels of Exhausted and Dysfunctional Phenotypes of Circulating CD161Frontiers in immunology · 2018Trial
- Allelic variation alters expression and antigen presentation of MR1 allomorphs.The Journal of biological chemistry · 2026Article
- Dual Roles of MAIT Cells in the Tumor Microenvironment: Implications for Cancer Immunity and Therapy.Immune network · 2026Review
- MR1-ligand cross-linking identifies vitamin B6 metabolites as TCR-reactive antigens.Cell reports methods · 2025Article
- Liver transplant-facilitated CD161Nature communications · 2025Article
- Cigarette smoke components modulate the MR1-MAIT axis.The Journal of experimental medicine · 2025Article
- MAIT cells: Conserved watchers on the wall.The Journal of experimental medicine · 2025Review
- Flavin and deazaflavin biosynthesis in mycobacteria: relevance to physiology, implications for drug discovery, MR-1 antigenicity, and vaccine development.Frontiers in immunology · 2025Review
- MR1 presents vitamin B6-related compounds for recognition by MR1-reactive T cells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Unraveling the phenotypic states of human innate-like T cells: Comparative insights with conventional T cells and mouse models.Cell reports · 2024Article
- Functional and biological implications of clonotypic diversity among human donor-unrestricted T cells.Immunology and cell biology · 2024Review
- Innate-like T cell subset commitment in the murine thymus is independent of TCR characteristics and occurs during proliferation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The MR1/MAIT cell axis in CNS diseases.Brain, behavior, and immunity · 2024Review
- Conserved allomorphs of MR1 drive the specificity of MR1-restricted TCRs.Frontiers in oncology · 2024Article
- Unraveling the Phenotypic States of Human innate-like T Cells: Comparative Insights with Conventional T Cells and Mouse Models.bioRxiv : the preprint server for biology · 2023Article
- Single-cell analysis of human MAIT cell transcriptional, functional and clonal diversity.Nature immunology · 2023Article
- Aging unconventionally: γδ T cells, iNKT cells, and MAIT cells in aging.Seminars in immunology · 2023Review
- Varicella Zoster Virus Impairs Expression of the Nonclassical Major Histocompatibility Complex Class I-Related Gene Protein (MR1).The Journal of infectious diseases · 2023Article
64 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
Abstract
Mucosal-associated invariant T (MAIT) cells express a semiinvariant αβ T cell receptor (TCR) that binds MHC class I-like molecule (MR1). However, the molecular basis for MAIT TCR recognition by MR1 is unknown. In this study, we present the crystal structure of a human Vα7.2Jα33-Vβ2 MAIT TCR. Mutagenesis revealed highly conserved requirements for the MAIT TCR-MR1 interaction across different human MAIT TCRs stimulated by distinct microbial sources. Individual residues within the MAIT TCR β chain were dispensable for the interaction with MR1, whereas the invariant MAIT TCR α chain controlled specificity through a small number of residues, which are conserved across species and located within the Vα-Jα regions. Mutagenesis of MR1 showed that only two residues, which were centrally positioned and on opposing sides of the antigen-binding cleft of MR1, were essential for MAIT cell activation. The mutagenesis data are consistent with a centrally located MAIT TCR-MR1 docking that was dominated by the α chain of the MAIT TCR. This candidate docking mode contrasts with that of the NKT TCR-CD1d-antigen interaction, in which both the α and β chain of the NKT TCR is required for ligation above the F'-pocket of CD1d.
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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.