Phage display of peptide/major histocompatibility complex
| Autor: | Bernard Piqueras, Jean-Marc Le Doussal, Guy Gorochov, Ismail Dogan, Patrice Debré |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Phage display
Protein Conformation Recombinant Fusion Proteins Immunology Antigen presentation Receptors Antigen T-Cell chemical and pharmacologic phenomena Peptide Major histocompatibility complex Epitope law.invention Epitopes Peptide Library law Escherichia coli Immunology and Allergy Peptide library chemistry.chemical_classification Antigen Presentation biology T-cell receptor H-2 Antigens Molecular biology Peptide Fragments DNA-Binding Proteins Solubility chemistry Periplasm biology.protein Recombinant DNA Capsid Proteins Oligopeptides Viral Fusion Proteins Protein Binding |
| Zdroj: | Journal of Immunological Methods. 241:147-158 |
| ISSN: | 0022-1759 |
| DOI: | 10.1016/s0022-1759(00)00211-8 |
| Popis: | To date, there is no direct way to determine the antigenic specificity of T-cells. While B-cell epitopes can be selected from phage-displayed libraries of peptides, the corresponding molecular tool for identifying T-cell epitopes does not yet exist. The natural ligands of the T-cell antigen-receptor (TCR) are essentially antigenic peptides (P) associated with the products of the major histocompatibility complex (MHC). Here, we report phages displaying P-MHC complexes. Single-chain P-MHC class I molecules, produced in E. coli periplasm, stimulate T-cells in a peptide-specific fashion. The same P-MHC, fused at the tip of filamentous phage, directed their binding to a recombinant TCR restricted to the displayed MHC haplotype (H-2K(d)). Importantly, the binding of P-K(d)-fd to a K(d)-restricted TCR, and also to K(d)-restricted T-cell hybridomas, was modulated by the displayed peptide. Therefore, we suggest phage display of P-MHC as a direct molecular tool for probing T-cell specificity, and for selecting TCR ligands from genetic libraries encoding randomized or natural peptides. |
| Databáze: | OpenAIRE |
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