ArticleMolecular therapy oncolytics2016
An MHC-restricted antibody-based chimeric antigen receptor requires TCR-like affinity to maintain antigen specificity.
Article in Molecular therapy oncolytics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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
60 citing papers in PubMed, 99 citations in OpenAlex.
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- Targeting intracellular LMP2 with costimulatory signal-armed antibody-like TCR T cells.JCI insight · 2025Article
- Nanobody-enhanced chimeric antigen receptor T-cell therapy: overcoming barriers in solid tumors with VHH and VNAR-based constructs.Biomarker research · 2025Review
- SynNotch CAR-T cell, when synthetic biology and immunology meet again.Frontiers in immunology · 2025Review
- Targeting of acute myeloid leukemia by five-gene engineered T cells expressing transgenic T-cell receptor specific to WT1, chimeric antigenic receptor specific to GM-CSF receptor, bispecific T-cell engager specific to CD33, and tEGFR suicide gene system.Immunotherapy advances · 2025Article
- TCR/CD3-based synthetic antigen receptors (TCC) convey superior antigen sensitivity combined with high fidelity of activation.Science advances · 2024Article
- Exploring the potential of the convergence between extracellular vesicles and CAR technology as a novel immunotherapy approach.Journal of extracellular biology · 2024Review
- CAR-T cell therapy: a game-changer in cancer treatment and beyond.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2024Review
- Regulation of temporal cytokine production by co-stimulation receptors in TCR-T cells is lost in CAR-T cells.Immunotherapy advances · 2024Article
- Harnessing antibody-mediated recognition of the intracellular proteome with T cell receptor-like specificity.Frontiers in immunology · 2024Review
- Using CombiCells, a platform for titration and combinatorial display of cell surface ligands, to study T-cell antigen sensitivity modulation by accessory receptors.The EMBO journal · 2024Article
- Hydrophobic interactions dominate the recognition of a KRAS G12V neoantigen.Nature communications · 2023Article
- The Current Status and Future Perspectives of Chimeric Antigen Receptor-Engineered T Cell Therapy for the Management of Patients with Endometrial Cancer.Current issues in molecular biology · 2023Review
- TCR-engineered T cell therapy in solid tumors: State of the art and perspectives.Science advances · 2023Review
- Inefficient exploitation of accessory receptors reduces the sensitivity of chimeric antigen receptors.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- ErbB- and MUC1-targeted CAR-T cell immunotherapy of oral squamous cell carcinoma.Frontiers in dental medicine · 2023Review
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
Chimeric antigen receptors (CARs) are synthetic receptors that usually redirect T cells to surface antigens independent of human leukocyte antigen (HLA). Here, we investigated a T cell receptor-like CAR based on an antibody that recognizes HLA-A*0201 presenting a peptide epitope derived from the cancer-testis antigen NY-ESO-1. We hypothesized that this CAR would efficiently redirect transduced T cells in an HLA-restricted, antigen-specific manner. However, we found that despite the specificity of the soluble Fab, the same antibody in the form of a CAR caused moderate lysis of HLA-A2 expressing targets independent of antigen owing to T cell avidity. We hypothesized that lowering the affinity of the CAR for HLA-A2 would improve its specificity. We undertook a rational approach of mutating residues that, in the crystal structure, were predicted to stabilize binding to HLA-A2. We found that one mutation (DN) lowered the affinity of the Fab to T cell receptor-range and restored the epitope specificity of the CAR. DN CAR T cells lysed native tumor targets
Identifiers
What OpenQuestion holds
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.