Carbohydrate Binding Specificity of Recombinant Human Macrophage β-Glucan Receptor Dectin-1

Abstract

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.