Directed Evolution of Human T-Cell Receptors with Picomolar Affinities by Phage Display  

Oleh:

Yi, Li ; Moysey, Ruth ; Molloy, Peter E. ; Vuidepot, Anne-Lise ; Mahon, Tara ; Baston, Emma ; Dunn, Steven ; Liddy, Nathaniel ; Jacob, Jansen ; Jakobsen, Bent K. ; Boulter, Jonathan M.

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: Nature Biotechnology: The Science and Business of Biotechnology vol. 23 no. 3 (Mar. 2005), page 349-354.
Topik: EVOLUTION; evolution; human T-Cell receptors; picomolar affinities; phage display

Ketersediaan

Perpustakaan Pusat (Semanggi) Nomor Panggil: NN9.2 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

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Isi artikel

Peptides derived from almost all protein, 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 1 - 100 uM. Here we describe the display of ten different human TCRs on the surface of bacteriophage, stabilized by a nonnative interchain disulfide bond. We report the directed evolution of high affinity TCRs specific for two different pHLAs, the human T-cell lymphotropic virus tye 1 (HTLV-1) tax (11-19) peptide-HLA-A*0,201 complex and the NY-ESO-I157-165) tumor associated peptide antigen-HLA-A*0,201 complex with affinities of up to 2,5nM and 26 pM, respectively and we demonstrate their high specificity and sensitivity for targeting of cell surface pHLAs.

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