Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 44 - 49 |
| Number of pages | 6 |
| Journal | Nature |
| Volume | 448 |
| Issue number | 7149 |
| Publication status | Published - 2007 |
Cite this
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CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor. / Borg, Natalie; Wun, Kwok Soon; Kjer-Nielsen, Lars; Wilce, Matthew Charles James; Pellicci, Daniel G; Koh, Ruide; Besra, Gurdyal S; Bharadwaj, Mandvi; Godfrey, Dale I; McCluskey, James; Rossjohn, Jamie.
In: Nature, Vol. 448, No. 7149, 2007, p. 44 - 49.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor
AU - Borg, Natalie
AU - Wun, Kwok Soon
AU - Kjer-Nielsen, Lars
AU - Wilce, Matthew Charles James
AU - Pellicci, Daniel G
AU - Koh, Ruide
AU - Besra, Gurdyal S
AU - Bharadwaj, Mandvi
AU - Godfrey, Dale I
AU - McCluskey, James
AU - Rossjohn, Jamie
PY - 2007
Y1 - 2007
N2 - The CD1 family is a large cluster of non-polymorphic, major histocompatibility complex (MHC) class-I-like molecules that bind distinct lipid-based antigens that are recognized by T cells. The most studied group of T cells that interact with lipid antigens are natural killer T (NKT) cells, which characteristically express a semi-invariant T-cell receptor (NKT TCR) that specifically recognizes the CD1 family member, CD1d. NKT-cell-mediated recognition of the CD1d?antigen complex has been implicated in microbial immunity, tumour immunity, autoimmunity and allergy. Here we describe the structure of a human NKT TCR in complex with CD1d bound to the potent NKT-cell agonist -galactosylceramide, the archetypal CD1d-restricted glycolipid. In contrast to T-cell receptor?peptide-antigen?MHC complexes, the NKT TCR docked parallel to, and at the extreme end of the CD1d-binding cleft, which enables a lock-and-key type interaction with the lipid antigen. The structure provides a basis for the interaction between the highly conserved NKT TCR -chain and the CD1d?antigen complex that is typified in innate immunity, and also indicates how variability of the NKT TCR -chain can impact on recognition of other CD1d?antigen complexes. These findings provide direct insight into how a T-cell receptor recognizes a lipid-antigen-presenting molecule of the immune system.
AB - The CD1 family is a large cluster of non-polymorphic, major histocompatibility complex (MHC) class-I-like molecules that bind distinct lipid-based antigens that are recognized by T cells. The most studied group of T cells that interact with lipid antigens are natural killer T (NKT) cells, which characteristically express a semi-invariant T-cell receptor (NKT TCR) that specifically recognizes the CD1 family member, CD1d. NKT-cell-mediated recognition of the CD1d?antigen complex has been implicated in microbial immunity, tumour immunity, autoimmunity and allergy. Here we describe the structure of a human NKT TCR in complex with CD1d bound to the potent NKT-cell agonist -galactosylceramide, the archetypal CD1d-restricted glycolipid. In contrast to T-cell receptor?peptide-antigen?MHC complexes, the NKT TCR docked parallel to, and at the extreme end of the CD1d-binding cleft, which enables a lock-and-key type interaction with the lipid antigen. The structure provides a basis for the interaction between the highly conserved NKT TCR -chain and the CD1d?antigen complex that is typified in innate immunity, and also indicates how variability of the NKT TCR -chain can impact on recognition of other CD1d?antigen complexes. These findings provide direct insight into how a T-cell receptor recognizes a lipid-antigen-presenting molecule of the immune system.
UR - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17581592
M3 - Article
VL - 448
SP - 44
EP - 49
JO - Nature
JF - Nature
SN - 0028-0836
IS - 7149
ER -