ArticleProceedings of the National Academy of Sciences of the United States of America2014
Molecular basis of mycobacterial lipid antigen presentation by CD1c and its recognition by αβ T cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 64 citations in OpenAlex.
- Human CD1c-autoreactive T-cells recogniseeLife · 2026Article
- Role of Donor Unrestricted T Cells (DURTs) in TB Host Defense: Implications for Novel TB Vaccine Development.Vaccines · 2026Review
- Sideways lipid presentation by the antigen-presenting molecule CD1c.Nature communications · 2025Article
- Structural insights into clonal restriction and diversity in T cell recognition of two immunodominant SARS-CoV-2 nucleocapsid epitopes.Nature communications · 2025Article
- Sideways lipid presentation by the antigen-presenting molecule CD1c.bioRxiv : the preprint server for biology · 2025Article
- Three-Dimensional Modeling ofAntibodies (Basel, Switzerland) · 2025Article
- The oral drug obeldesivir protects nonhuman primates against lethal Ebola virus infection.Science advances · 2025Article
- CD1-restricted T cells: are unconventional allies the key to future TB vaccines?Frontiers in immunology · 2025Review
- A CD1c lipid agnostic T cell receptor bispecific engager redirects T cells against CD1cFrontiers in immunology · 2025Article
- Neoantigens: new hope for cancer therapy.Frontiers in oncology · 2025Review
- A conserved human CD4+ T cell subset recognizing the mycobacterial adjuvant trehalose monomycolate.The Journal of clinical investigation · 2024Article
- Optimizing iNKT-driven immune responses against cancer by modulating CD1d in tumor and antigen presenting cells.Clinical immunology (Orlando, Fla.) · 2024Review
- Immature B cell homing shapes human lymphoid tissue structure and function.The Journal of experimental medicine · 2024Article
- A structural perspective of how T cell receptors recognize the CD1 family of lipid antigen-presenting molecules.The Journal of biological chemistry · 2024Review
- Functional and biological implications of clonotypic diversity among human donor-unrestricted T cells.Immunology and cell biology · 2024Review
- CD1a and bound lipids drive T-cell responses in human skin disease.European journal of immunology · 2023Review
- Unconventional T cells and kidney disease.Nature reviews. Nephrology · 2021Review
- Intrathymic differentiation of natural antibody-producing plasma cells in human neonates.Nature communications · 2021Article
- Article
- Chemical Synthesis of Cell Wall Constituents ofChemical reviews · 2021Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
CD1c is a member of the group 1 CD1 family of proteins that are specialized for lipid antigen presentation. Despite high cell surface expression of CD1c on key antigen-presenting cells and the discovery of its mycobacterial lipid antigen presentation capability, the molecular basis of CD1c recognition by T cells is unknown. Here we present a comprehensive functional and molecular analysis of αβ T-cell receptor (TCR) recognition of CD1c presenting mycobacterial phosphomycoketide antigens. Our structure of CD1c with the mycobacterial phosphomycoketide (PM) shows similarities to that of CD1c-mannosyl-β1-phosphomycoketide in that the A' pocket accommodates the mycoketide alkyl chain; however, the phosphate head-group of PM is shifted ∼6 Å in relation to that of mannosyl-β1-PM. We also demonstrate a bona fide interaction between six human TCRs and CD1c-mycoketide complexes, measuring high to moderate affinities. The crystal structure of the DN6 TCR and mutagenic studies reveal a requirement of five complementarity determining region (CDR) loops for CD1c recognition. Furthermore, mutagenesis of CD1c reveals residues in both the α1 and α2 helices involved in TCR recognition, yet not entirely overlapping among the examined TCRs. Unlike patterns for MHC I, no archetypical binding footprint is predicted to be shared by CD1c-reactive TCRs, even when recognizing the same or similar antigens.
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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.