ArticleJournal of immunological methods2013
Engineering improved T cell receptors using an alanine-scan guided T cell display selection system.
Article in Journal of immunological methods, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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
26 citing papers in PubMed, 36 citations in OpenAlex.
- TCR-FramePose: a local-frame representation for decomposing global docking and CDR3 loop geometry in TCR-pMHC recognition.bioRxiv : the preprint server for biology · 2026Article
- Current developments in T-cell receptor therapy for acute myeloid leukemia.Blood advances · 2025Review
- In situ cell-surface conformation of the TCR-CD3 signaling complex.EMBO reports · 2024Article
- Novel insights into TCR-T cell therapy in solid neoplasms: optimizing adoptive immunotherapy.Experimental hematology & oncology · 2024Review
- Advancements in mammalian display technology for therapeutic antibody development and beyond: current landscape, challenges, and future prospects.Frontiers in immunology · 2024Review
- Strategies and rules for tuning TCR-derived therapy.Expert reviews in molecular medicine · 2023Review
- Challenges and solutions for therapeutic TCR-based agents.Immunological reviews · 2023Review
- Engineering soluble T-cell receptors for therapy.The FEBS journal · 2021Review
- An HLA-A*11:01-Binding Neoantigen from Mutated NPM1 as Target for TCR Gene Therapy in AML.Cancers · 2021Article
- Avidity optimization of a MAGE-A1-specific TCR with somatic hypermutation.European journal of immunology · 2021Article
- Review
- Review
- Stabilization of soluble high-affinity T-cell receptor with de novo disulfide bonds.FEBS letters · 2020Article
- Empirical and Rational Design of T Cell Receptor-Based Immunotherapies.Frontiers in immunology · 2020Review
- T-cell Receptors EngineeredCancer immunology research · 2019Article
- Human cytomegalovirus-specific T-cell receptor engineered for high affinity and soluble expression using mammalian cell display.The Journal of biological chemistry · 2019Article
- Weaponizing T-cell receptors through molecular engineering.The Journal of biological chemistry · 2019Article
- Molecular properties of gp100-reactive T-cell receptors drive the cytokine profile and antitumor efficacy of transgenic host T cells.Pigment cell & melanoma research · 2019Article
- Critical biological parameters modulate affinity as a determinant of function in T-cell receptor gene-modified T-cells.Cancer immunology, immunotherapy : CII · 2017Article
- Structural Model of the Extracellular Assembly of the TCR-CD3 Complex.Cell reports · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
T cell receptors (TCRs) on T cells recognize peptide-major histocompatibility complex (pMHC) molecules on the surface of antigen presenting cells and this interaction determines the T cell immune response. Due to negative selection, naturally occurring TCRs bind self (tumor) peptides with low affinity and have a much higher affinity for foreign antigens. This complicates isolation of naturally occurring, high affinity TCRs that mediate more effective tumor rejection for therapeutic purposes. An attractive approach to resolve this issue is to engineer high affinity TCRs in vitro using phage, yeast or mammalian TCR display systems. A caveat of these systems is that they rely on a large library by random mutagenesis due to the lack of knowledge regarding the specific interactions between the TCR and pMHC. We have focused on the mammalian retroviral display system because it uniquely allows for direct comparison of TCR-pMHC-binding properties with T-cell activation outcomes. Through an alanine-scanning approach, we are able to quickly map the key amino acid residues directly involved in TCR-pMHC interactions thereby significantly reducing the library size. Using this method, we demonstrate that for a self-antigen-specific human TCR (R6C12) the key residues for pMHC binding are located in the CDR3β region. This information was used as a basis for designing an efficacious TCR CDR3α library that allowed for selection of TCRs with higher avidity than the wild-type as evaluated through binding and activation experiments. This is a direct approach to target specific TCR residues in TCR library design to efficiently engineer high avidity TCRs that may potentially be used to enhance adoptive immunotherapy treatments.
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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.