Engineered T-Cell Receptor Tetramers Bind MHC - Peptide Complexes with High Affinity  

Oleh:

Subbramanian, Ramu A. ; Moriya, Chikaya ; Martin, Kristi L. ; Peyerl, Fred W. ; Hasegawa, Atsuhiko ; Naoi, Akira ; Chhay, Heng ; Autissier, Patrick ; Gorgone, Darci A. ; Lifton, Michelle A. ; Kuus-Reichel, Kristine ; Schmitz, Jorn E. ; Letvin, Norman L. ; Kuroda, Marcelo J.

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: Nature Biotechnology: The Science and Business of Biotechnology vol. 22 no. 11 (Nov. 2004), page 1429-1434.
Topik: CELL; t-cell receptor; tetraers; MHC-peptide; affinity

Ketersediaan

Perpustakaan Pusat (Semanggi) Nomor Panggil: NN9.3 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

Lihat Detail Induk

Isi artikel

In this study we extend tetramerization technology to T-cell receptors (TCRs). We identified TCR ab pairs in the absence of accessory molecules, ensuring isolation of high-affinity TCRs that maintain stable binding characteristics after tetramerization. Subtle changes in cognate peptide levels bound to the class I molecule were accurately reflected by parallel changes in the mean fluorescence intensity of cells that bound TCR tetramers, allowing us to accurately assess the binding affinity of a panel of peptides to major histocompatibility complex (MHC) class I. Using a TCR tetramer specific for the Mamu A 01 allele, we identified animals expressing this restricting class I allele from a large cohort of outbred rhesus macaques. TCR tetramers should facilitate analysis of the MHC peptide interface and more generally, the design of immunotherapeutics and vaccines.

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