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Specific increase in potency via structure-based design of a TCR.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Johnson, Laura A. Cardozo, Timothy Grigoryan, Arsen Gu, Wei Jun Krogsgaard, Michelle Zhong, Shi Malecek, Karolina Rosenberg, Steven A.
Description	Author Affiliation: Malecek K ( Perlmutter Cancer Center, New York University School of Medicine, New York, NY 10016); Grigoryan A ( Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016); Zhong S ( Perlmutter Cancer Center, New York University School of Medicine, New York, NY 10016); Gu WJ ( Department of Chemistry, New York University, New York, NY 10012); Johnson LA ( Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892); Rosenberg SA ( Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892); Cardozo T ( Perlmutter Cancer Center, New York University School of Medicine, New York, NY 10016); Krogsgaard M ( Perlmutter Cancer Center, New York University School of Medicine, New York, NY 10016)
Abstract	Adoptive immunotherapy with Ag-specific T lymphocytes is a powerful strategy for cancer treatment. However, most tumor Ags are nonreactive 'self' proteins, which presents an immunotherapy design challenge. Recent studies have shown that tumor-specific TCRs can be transduced into normal PBLs, which persist after transfer in â ¼30% of patients and effectively destroy tumor cells in vivo. Although encouraging, the limited clinical responses underscore the need for enrichment of T cells with desirable antitumor capabilities prior to patient transfer. In this study, we used structure-based design to predict point mutations of a TCR (DMF5) that enhance its binding affinity for an agonist tumor Ag-MHC (peptide-MHC [pMHC]), Mart-1 (27L)-HLA-A2, which elicits full T cell activation to trigger immune responses. We analyzed the effects of selected TCR point mutations on T cell activation potency and analyzed cross-reactivity with related Ags. Our results showed that the mutated TCRs had improved T cell activation potency while retaining a high degree of specificity. Such affinity-optimized TCRs have demonstrated to be very specific for Mart-1 (27L), the epitope for which they were structurally designed. Although of somewhat limited clinical relevance, these studies open the possibility for future structural-based studies that could potentially be used in adoptive immunotherapy to treat melanoma while avoiding adverse autoimmunity-derived effects.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1302344
Journal	The Journal of Immunology
Issue Number	5
Volume Number	193
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2014-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Epitopes, T-lymphocyte Mart-1 Antigen Peptides Protein Engineering Receptors, Antigen, T-cell Animals Cell Line, Tumor Chemistry Genetics Immunology Lymphocyte Activation Point Mutation Structure-activity Relationship Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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Specific roles of each TCR hemichain in generating functional chain-centric TCR.

Death receptor-independent activation-induced cell death in human melanoma antigen-specific MHC class I-restricted TCR-engineered CD4 T cells.

Rapid and selective expansion of nonclonotypic T cells in regulatory T cell-deficient, foreign antigen-specific TCR-transgenic scurfy mice: antigen-dependent expansion and TCR analysis.

The TCR repertoires of regulatory and conventional T cells specific for the same foreign antigen are distinct.

Enhanced TCR footprint by a novel glycolipid increases NKT-dependent tumor protection.

Transcriptional profile of tuberculosis antigen-specific T cells reveals novel multifunctional features.

Cutting Edge: CD1a tetramers and dextramers identify human lipopeptide-specific T cells ex vivo.

Dengue virus specific dual HLA binding T cell epitopes induce CD8+ T cell responses in seropositive individuals.

SNX17 affects T cell activation by regulating TCR and integrin recycling.

Specific increase in potency via structure-based design of a TCR.

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Specific increase in potency via structure-based design of a TCR.