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International Immunology, Vol. 13, No. 7, 853-861, July 2001
© 2001 Japanese Society for Immunology

Crucial amino acid residues of mouse CD1d for glycolipid ligand presentation to V{alpha}14 NKT cells

Noriaki Kamada1,2, Hiroshi Iijima3, Kaname Kimura3, Michishige Harada1, Eiko Shimizu1, Shin-ichiro Motohashi1, Tetsu Kawano1, Hiroshi Shinkai2, Toshinori Nakayama1, Teruyuki Sakai3, Laurent Brossay4, Mitchell Kronenberg4 and Masaru Taniguchi1 1 CREST (Core Research for Evolutional Science and Technology) and Department of Molecular Immunology, Graduate School of Medicine, and
2 Department of Dermatology, School of Medicine, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba 260-8670, Japan
3 Pharmaceutical Research Laboratory, Kirin Brewery Co., Ltd, 3 Miyahara, Gunma 370-12, Japan
4 La Jolla Institute for Allergy and Immunology, 10355 Science Center Drive, San Diego, CA 92121, USA

Correspondence to: M. Taniguchi

A novel lymphocyte, NKT cells bearing an invariant V{alpha}14 antigen receptor, specifically recognizes {alpha}-galactosylceramide ({alpha}-GalCer) exclusively presented by mouse CD1d (mCD1d). However, the precise molecular interaction remains unclear. For the basis of functional analyses, a docking model of {alpha}-GalCer with the crystal structure of mCD1d was constructed. Possible residues involved in the {alpha}-GalCer–mCD1d interaction were found to be Arg79, Glu83 and Asp80 for carbohydrate recognition, and Asp153 for interaction with the amide group on the fatty acyl chain. The {alpha}-GalCer-presenting ability of various transfectants expressing mutant mCD1d was completely abrogated if a single amino acid mutation was induced at positions 79, 80, 83 or 153, suggesting that the polar amino acids above the F' pocket are crucial for {alpha}-GalCer presentation to activate V{alpha}14 NKT cells. The possibility that Glu83 is a contact site for the NKT cell receptor is also discussed.

Keywords: {alpha}-galactosylceramide, NKT cell receptor, docking modeling

The first two authors contributed equally to this work

Transmitting editor: M. Miyasaka


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