A novel recognition motif of human NKT antigen receptor for a glycolipid ligand
| Autor: | Eiko Shimizu, Yujiro Tanaka, Hiroshi Sato, Noriaki Kamata, Hisao Osada, Yoshikatsu Kaneko, Masaru Taniguchi, Tetsu Kawano, Toshinori Nakayama, Soei Sekiya |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Adult
Receptors Antigen T-Cell alpha-beta T cell Immunology Galactosylceramides chemical and pharmacologic phenomena Complementarity determining region Ligands Lymphocyte Activation Antigens CD1 Mice Glycolipid Antigen T-Lymphocyte Subsets medicine Animals Humans Immunology and Allergy Receptor Binding Sites biology General Medicine Fetal Blood Natural killer T cell Molecular biology Killer Cells Natural medicine.anatomical_structure Polyclonal antibodies CD1D biology.protein lipids (amino acids peptides and proteins) Antigens CD1d |
| Zdroj: | International Immunology. 11:881-887 |
| ISSN: | 1460-2377 |
| DOI: | 10.1093/intimm/11.6.881 |
| Popis: | 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 Valpha24(+)Vbeta11(+) cells, functionally defining the human NKT cells. The naive human NKT cell repertoire consisted of cells expressing an invariant Valpha24JalphaQ chain and a diverse array of beta chains derived from a single Vbeta11 gene segment. Stimulation with alpha-GalCer expanded a polyclonal subset of the human NKT cell repertoire carrying a novel complementarity-determining region (CDR) 3beta consensus motif that may directly interact with the sugar moiety of alpha-GalCer. Our data suggest that certain redundancy is allowed for CDR3beta of NKT antigen receptor to interact with the ligand and provide a first clue to understand the novel protein-carbohydrate interaction mechanisms. |
| Databáze: | OpenAIRE |
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