ArticleJournal of immunology (Baltimore, Md. : 1950)2020
Structure of MHC-Independent TCRs and Their Recognition of Native Antigen CD155.
Article in Journal of immunology (Baltimore, Md. : 1950), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The trial behind it
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Direct recognition of an intact foreign protein by an αβ T cell receptor.Nature communications · 2024Article
- SARS-CoV-2 spike does not interact with the T cell receptor or directly activate T cells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Selection, engineering, and in vivo testing of a human leukocyte antigen-independent T-cell receptor recognizing human mesothelin.PloS one · 2024Article
- A conserved element in the first intron ofFrontiers in immunology · 2024Article
- Renal tubular epithelial cells are constitutive non-cognate stimulators of resident T cells.Cell reports · 2023Article
- MHC-independent αβT cells: Lessons learned about thymic selection and MHC-restriction.Frontiers in immunology · 2022Review
- Novel MHC-Independent αβTCRs Specific for CD48, CD102, and CD155 Self-Proteins and Their Selection in the Thymus.Frontiers in immunology · 2020Article
- Coreceptors and TCR Signaling - the Strong and the Weak of It.Frontiers in cell and developmental biology · 2020Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
During normal T cell development in the thymus, αβ TCRs signal immature thymocytes to differentiate into mature T cells by binding to peptide-MHC ligands together with CD4/CD8 coreceptors. Conversely, in MHC and CD4/CD8 coreceptor-deficient mice, the thymus generates mature T cells expressing MHC-independent TCRs that recognize native conformational epitopes rather than linear antigenic-peptides presented by MHC. To date, no structural information of MHC-independent TCRs is available, and their structural recognition of non-MHC ligand remains unknown. To our knowledge in this study, we determined the first structures of two murine MHC-independent TCRs (A11 and B12A) that bind with high nanomolar affinities to mouse adhesion receptor CD155. Solution binding demonstrated the Vαβ-domain is responsible for MHC-independent B12A recognition of its ligand. Analysis of A11 and B12A sequences against various MHC-restricted and -independent TCR sequence repertoires showed that individual V-genes of A11 and B12A did not exhibit preference against MHC-restriction. Likewise, CDR3 alone did not discriminate against MHC binding, suggesting VDJ recombination together with Vα/Vβ pairing determine their MHC-independent specificity for CD155. The structures of A11 and B12A TCR are nearly identical to those of MHC-restricted TCR, including the conformations of CDR1 and 2. Mutational analysis, together with negative-staining electron microscopy images, showed that the CDR regions of A11 and B12A recognized epitopes on D1 domain of CD155, a region also involved in CD155 binding to poliovirus and Tactile in human. Taken together, MHC-independent TCRs adopt canonical TCR structures to recognize native Ags, highlighting the importance of thymic selection in determining TCR ligand specificity.
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Registered trials
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