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- Title
Engineered T-cell receptor tetramers bind MHC-peptide complexes with high affinity.
- Authors
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, Jörn E.; Letvin, Norman L.; Kuroda, Marcelo J.
- Abstract
In this study we extend tetramerization technology to T-cell receptors (TCRs). We identified TCRaßpairs 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.
- Subjects
MAJOR histocompatibility complex; T-cell receptor genes; FLUORESCENCE; RHESUS monkeys; VACCINES; IMMUNOGENETICS
- Publication
Nature Biotechnology, 2004, Vol 22, Issue 11, p1429
- ISSN
1087-0156
- Publication type
Article
- DOI
10.1038/nbt1024