Crystal Structure of Vδ1T Cell Receptor in Complex with CD1d-Sulfatide Shows MHC-like Recognition of a Self-Lipid by Human γδ T Cells

Adrienne M. Luoma, Caitlin D. Castro, Toufic Mayassi, Leslie A. Bembinster, Li Bai, Damien Picard, Brian Anderson, Louise Scharf, Jennifer E. Kung, Leah V. Sibener, Paul B. Savage, Bana Jabri, Albert Bendelac, Erin J. Adams

Research output: Contribution to journalArticlepeer-review

191 Scopus citations

Abstract

The nature of the antigens recognized by γδ Tcells 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 Tcells, 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 Tcells. These findings provide structural demonstration of MHC-like recognition of a self-lipid by γδ Tcells and reveal the prevalence of lipid recognition by innate-like T cell populations.

Original languageEnglish
Pages (from-to)1032-1042
Number of pages11
JournalImmunity
Volume39
Issue number6
DOIs
StatePublished - 12 Dec 2013
Externally publishedYes

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