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A novel recognition motif of human NKT antigen receptor for a glycolipid ligand
被引:52
作者:
Kawano, T
Tanaka, Y
Shimizu, E
Kaneko, Y
Kamata, N
Sato, H
Osada, H
Sekiya, S
Nakayama, T
Taniguchi, M
机构:
[1] Chiba Univ, CREST, Chuo Ku, Chiba 2608670, Japan
[2] Chiba Univ, Dept Mol Immunol, Chuo Ku, Chiba 2608670, Japan
[3] Chiba Univ, Grad Sch Med, Dept Dev Immunol, Chuo Ku, Chiba 2608670, Japan
[4] Chiba Univ, Sch Med, Dept Obstet & Gynaecol, Chuo Ku, Chiba 2608670, Japan
关键词:
carbohydrate-binding proteins;
complementarity-determining region;
NKT antigen receptor;
protein-sugar interaction;
repertoire selection;
D O I:
10.1093/intimm/11.6.881
中图分类号:
R392 [医学免疫学];
Q939.91 [免疫学];
学科分类号:
100102 ;
摘要:
Murine NKT cells can recognize a-galactosylceramide (alpha-GalCer) in the context of a class Ib CD1d molecule. Here we show that alpha-GalCer can selectively activate freshly isolated human V(alpha)24(+)V(beta)11 (+) cells, functionally defining the human NKT cells. The naive human NKT cell repertoire consisted of cells expressing an invariant V(alpha)24J(alpha)Q chain and a diverse array of beta chains derived from a single V beta 11 gene segment. Stimulation with a-GalCer expanded a polyclonal subset of the human NKT cell repertoire carrying a novel complementarity-determining region (CDR) 3 beta consensus motif that may directly interact with the sugar moiety of a-GalCer, Our data suggest that certain redundancy is allowed for CDR3 beta of NKT antigen receptor to interact with the ligand and provide a first clue to understand the novel protein-carbohydrate interaction mechanisms.
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页码:881 / 887
页数:7
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