期刊
NATURE BIOTECHNOLOGY
卷 23, 期 3, 页码 349-354出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nbt1070
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Peptides derived from almost all proteins, including disease-associated proteins, can be presented on the cell surface as peptide-human leukocyte antigen (pHLA) complexes. T cells specifically recognize pHLA with their clonally rearranged T-cell receptors (TCRs), whose natural affinities are limited to similar to 1-100 mu M-1. Here we describe the display of ten different human TCRs on the surface of bacteriophage, stabilized by a nonnative interchain disulfide bond(2). We report the directed evolution of high-affinity TCRs specific for two different pHLAs: the human T-cell lymphotropic virus type 1 (HTLV-1) tax(11-19) peptide-HLA-A*0201 complex(3) and the NY-ESO-1(157-165) tumor-associated peptide antigen-HLA-A*0201 complex(4), with affinities of up to 2.5 nM and 26 pM, respectively, and we demonstrate their high specificity and sensitivity for targeting of cell-surface pHLAs.
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