Format

Send to

Choose Destination
Immunity. 2013 Dec 12;39(6):1032-42. doi: 10.1016/j.immuni.2013.11.001. Epub 2013 Nov 14.

Crystal structure of Vδ1 T cell receptor in complex with CD1d-sulfatide shows MHC-like recognition of a self-lipid by human γδ T cells.

Author information

1
Committee on Immunology, University of Chicago, Chicago, IL 60637, USA; Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
2
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
3
Committee on Immunology, University of Chicago, Chicago, IL 60637, USA; Department of Medicine, University of Chicago, Chicago, IL 60637, USA.
4
Institute of Immunology, School of Life Sciences, University of Science and Technology of China, Hefei 230027, China; Department of Pathology, University of Chicago, Chicago, IL 60637, USA; Howard Hughes Medical Institute.
5
Department of Pathology, University of Chicago, Chicago, IL 60637, USA; Howard Hughes Medical Institute.
6
Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, USA.
7
Committee on Immunology, University of Chicago, Chicago, IL 60637, USA; Department of Pathology, University of Chicago, Chicago, IL 60637, USA; Howard Hughes Medical Institute.
8
Committee on Immunology, University of Chicago, Chicago, IL 60637, USA; Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA. Electronic address: ejadams@uchicago.edu.

Abstract

The nature of the antigens recognized by γδ T cells and their potential recognition of major histocompatibility complex (MHC)-like molecules has remained unclear. Members of the CD1 family of lipid-presenting molecules are suggested ligands for Vδ1 TCR-expressing γδ T cells, the major γδ lymphocyte population in epithelial tissues. We crystallized a Vδ1 TCR in complex with CD1d and the self-lipid sulfatide, revealing the unusual recognition of CD1d by germline Vδ1 residues spanning all complementarity-determining region (CDR) loops, as well as sulfatide recognition separately encoded by nongermline CDR3δ residues. Binding and functional analysis showed that CD1d presenting self-lipids, including sulfatide, was widely recognized by gut Vδ1+ γδ T cells. These findings provide structural demonstration of MHC-like recognition of a self-lipid by γδ T cells and reveal the prevalence of lipid recognition by innate-like T cell populations.

PMID:
24239091
PMCID:
PMC3875342
DOI:
10.1016/j.immuni.2013.11.001
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center