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Dectin-1 is a major beta-glucan receptor on macrophages

By Gordon D. Brown, Philip Russel Taylor, Delyth M. Reid, Janet A. Willment, David L. Williams, Luisa Martinez-Pomares, Simon Y. C. Wong and Siamon Gordon


Zymosan is a ?-glucan– and mannan-rich particle that is widely used as a cellular activator for examining the numerous responses effected by phagocytes. The macrophage mannose receptor (MR) and complement receptor 3 (CR3) have historically been considered the major macrophage lectins involved in the nonopsonic recognition of these yeast-derived particles. Using specific carbohydrate inhibitors, we show that a ?-glucan receptor, but not the MR, is a predominant receptor involved in this process. Furthermore, nonopsonic zymosan binding was unaffected by genetic CD11b deficiency or a blocking monoclonal antibody (mAb) against CR3, demonstrating that CR3 was not the ?-glucan receptor mediating this activity. To address the role of the recently described ?-glucan receptor, Dectin-1, we generated a novel anti–Dectin-1 mAb, 2A11. Using this mAb, we show here that Dectin-1 was almost exclusively responsible for the ?-glucan–dependent, nonopsonic recognition of zymosan by primary macro-phages. These findings define Dectin-1 as the leukocyte ?-glucan receptor, first described over 50 years ago, and resolves the long-standing controversy regarding the identity of this important molecule. Furthermore, these results identify Dectin-1 as a new target for examining the immunomodulatory properties of ?-glucans for therapeutic drug design

Topics: QR, R1, RB
Publisher: Rockefeller University Press
Year: 2002
OAI identifier: oai:

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