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Carbohydrate binding specificity of recombinant human macrophage beta-glucan receptor dectin-1

Human macrophage dectin-1, a type II transmembrane β-glucan receptor, was expressed as a fusion protein with an N-terminal hexahistidine tag and glutathione S-transferase in an Escherichia coli cell-free translation system, and assayed for binding specificity. Recombinant dectin-1 specifically bound...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2009-01, Vol.73 (1), p.237-240
Main Authors: Ujita, M.(Meijo Univ., Nagoya (Japan). Faculty of Agriculture), Nagayama, H, Kanie, S, Koike, S, Ikeyama, Y, Ozaki, T, Okumura, H
Format: Article
Language:English
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Summary:Human macrophage dectin-1, a type II transmembrane β-glucan receptor, was expressed as a fusion protein with an N-terminal hexahistidine tag and glutathione S-transferase in an Escherichia coli cell-free translation system, and assayed for binding specificity. Recombinant dectin-1 specifically bound to some β-glucans, but not to other carbohydrates. The β-glucan binding of recombinant dectin-1 was inhibited by laminarin, a soluble β-glucan, and by laminarioligosaccharides, but not by other carbohydrates. These results suggest that recombinant human dectin-1 can be used as a useful probe in identifying ligands in humans and tonic foods due to its strict binding specificity.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.80503