期刊
JOURNAL OF IMMUNOLOGICAL METHODS
卷 241, 期 1-2, 页码 147-158出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0022-1759(00)00211-8
关键词
major histocompatibility complex; T-cell receptor; peptide; phage display
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. (C) 2000 Elsevier Science BN. All rights reserved.
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