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International Immunology, Vol. 11, No. 6, 881-887, June 1999
© 1999 Japanese Society for Immunology

A novel recognition motif of human NKT antigen receptor for a glycolipid ligand

Tetsu Kawano, Yujiro Tanaka1, Eiko Shimizu, Yoshikatsu Kaneko, Noriaki Kamata, Hiroshi Sato, Hisao Osada2, Soei Sekiya2, Toshinori Nakayama and Masaru Taniguchi

CREST (Core Research for Evolutional Science and Technology) Project and Department of Molecular Immunology,
1 Department of Developmental Immunology, Graduate School of Medicine, and
2 Department of Obstetrics and Gynaecology, School of Medicine, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba 260-8670, Japan

Correspondence to: M Taniguchi

Murine NKT cells can recognize {alpha}-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+Vß11+ 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 ß chains derived from a single Vß11 gene segment. Stimulation with {alpha}-GalCer expanded a polyclonal subset of the human NKT cell repertoire carrying a novel complementarity-determining region (CDR) 3ß consensus motif that may directly interact with the sugar moiety of {alpha}-GalCer. Our data suggest that certain redundancy is allowed for CDR3ß of NKT antigen receptor to interact with the ligand and provide a first clue to understand the novel protein–carbohydrate interaction mechanisms.

Keywords: carbohydrate-binding proteins, complementarity-determining region, NKT antigen receptor, protein–sugar interaction, repertoire selection

Transmitting editor: T. Watanabe


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