ArticleFrontiers in immunology2022
Computationally profiling peptide:MHC recognition by T-cell receptors and T-cell receptor-mimetic antibodies.
Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Structural T-Cell Receptor Analysis in the Age of Machine Learning.Immunological reviews · 2026Review
- Safety-first TCR-T: AI-guided specificity, base-editing to prevent mispairing, and prioritizing public neoantigens.Frontiers in immunology · 2026Article
- Article
- STCRpy: a software suite for T-cell receptor structure parsing, interaction profiling, and machine learning dataset preparation.Bioinformatics (Oxford, England) · 2025Article
- T-cell receptor structures and predictive models reveal comparable alpha and beta chain structural diversity despite differing genetic complexity.Communications biology · 2025Article
- Experimental Structures of Antibody/MHC-I Complexes Reveal Details of Epitopes Overlooked by Computational Prediction.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- A comparison of clustering models for inference of T cell receptor antigen specificity.Immunoinformatics (Amsterdam, Netherlands) · 2024Article
- Quantifying conformational changes in the TCR:pMHC-I binding interface.Frontiers in immunology · 2024Article
- Experimental structures of antibody/MHC-I complexes reveal details of epitopes overlooked by computational prediction.bioRxiv : the preprint server for biology · 2023Article
- Advances in vaccine development for cancer prevention and treatment in Lynch Syndrome.Molecular aspects of medicine · 2023Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
T-cell receptor-mimetic antibodies (TCRms) targeting disease-associated peptides presented by Major Histocompatibility Complexes (pMHCs) are set to become a major new drug modality. However, we lack a general understanding of how TCRms engage pMHC targets, which is crucial for predicting their specificity and safety. Several new structures of TCRm:pMHC complexes have become available in the past year, providing sufficient initial data for a holistic analysis of TCRms as a class of pMHC binding agents. Here, we profile the complete set of TCRm:pMHC complexes against representative TCR:pMHC complexes to quantify the TCR-likeness of their pMHC engagement. We find that intrinsic molecular differences between antibodies and TCRs lead to fundamentally different roles for their heavy/light chains and Complementarity-Determining Region loops during antigen recognition. The idiotypic properties of antibodies may increase the likelihood of TCRms engaging pMHCs with less peptide selectivity than TCRs. However, the pMHC recognition features of some TCRms, including the two TCRms currently in clinical trials, can be remarkably TCR-like. The insights gained from this study will aid in the rational design and optimisation of next-generation TCRms.
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