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

• 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
• Subjects: beta-Glucans - metabolism; binding specificity; Biological and medical sciences; Carbohydrates; dectin-1; ELECTROFORESIS; ELECTROPHORESE; ELECTROPHORESIS; ESCHERICHIA COLI; Fundamental and applied biological sciences. Psychology; GENERO HUMANO; GENRE HUMAIN; GLUCANE; GLUCANOS; GLUCANS; Glutathione Transferase; Humans; IMMUNOBLOTTING; immunostimulating activity; Lectins, C-Type; MACROFAGOS; MACROPHAGE; MACROPHAGES; Macrophages - chemistry; MANKIND; Membrane Proteins - metabolism; Molecular Probe Techniques; Nerve Tissue Proteins - metabolism; Protein Binding; PURIFICACION; PURIFICATION; RECEPTEURS; RECEPTOR; Receptors, Immunologic - metabolism; Recombinant Fusion Proteins - biosynthesis; β-glucan receptor
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.80503

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.