Receptor Binding of Fungal Cell Wall (1→3)-β-D-Glucan to Human Macrophage and Neutrophil Cell Lines

Document Type

Conference Proceeding

Publication Date

12-1-1999

Description

Herein, we will review the evidence for the binding of fungal derived (1→3)-β-D-glucans to receptors on human macrophage U937 and neutrophil HL-60 cell lines. We have observed binding of yeast derived (1→3)-β-D-glucan to multiple receptors in each cell line. We have also demonstrated that the receptor(s) is specific for (1→3)-β-D-glucan binding, since it will not recognize mannan or dextran, non-β linked polymers. In addition, the receptor(s) show dramatic differences in binding affinity between (1→3)-β-D-glucans. Scleroglucan a triple helical polymer binds with high affinity (IC50 = 23 nM), while single helical glucans, such as glucan phosphate and laminarin, are bound with lower affinity (IC50 = 24 μM). Our data indicate that human macrophage and neutrophil cell lines have multiple receptors which specifically bind (1→3)-β-D-glucans and that the triple helical conformation, molecular weight and polymer charge may be important determinants in receptor ligand interaction.

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