Article abstract
Nature Immunology 9, 777 - 784 (2008)
Published online: 30 May 2008 | doi:10.1038/ni.1620
An autonomous CDR3
is sufficient for recognition of the nonclassical MHC class I molecules T10 and T22 by 
T cells
Erin J Adams1, Pavel Strop2, Sunny Shin3, Yueh-Hsiu Chien3 & K Christopher Garcia2,4
Abstract
It remains unclear whether 
T cell antigen receptors (TCRs) detect antigens in a way similar to antibodies or 
TCRs. Here we show that reactivity between the G8 and KN6 TCRs and the major histocompatibility complex class Ib molecule T22 could be recapitulated, with retention of wild-type ligand affinity, in an TCR after grafting of a G8 or KN6 complementarity-determining region 3- (CDR3) loop in place of the CDR3 loop of an TCR. We also found that a shared sequence motif in CDR3 loops of all T22-reactive TCRs bound T22 in energetically distinct ways, and that T10d, which bound G8 with weak affinity, was converted into a high-affinity ligand by a single point mutation. Our results demonstrate unprecedented autonomy of a single CDR3 loop in antigen recognition.
- Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA.
- Department of Molecular and Cellular Physiology and Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, USA.
- Department of Microbiology & Immunology and Program in Immunology, Stanford University School of Medicine, Stanford, California 94305, USA.
- Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305, USA.
Correspondence to: Erin J Adams1 e-mail: ejadams@uchicago.edu
Correspondence to: K Christopher Garcia2,4 e-mail: kcgarcia@stanford.edu
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