The phagocytosis of pathogens is a critical event in host defense, not only for clearance of the invading microorganism, but also for the subsequent immune response. We have examined Dectin-1, a proinflammatory nonopsonic receptor for β-glucans, and show that it mediates the internalization of β-glucan-bearing ligands, including yeast particles. Although requiring tyrosine phosphorylation and the cytoplasmic immunoreceptor tyrosine-based activation motif (ITAM)-like motif, uptake mediated by Dectin-1 was different from any previously reported phagocytic receptor and was not dependent on Syk-kinase in macrophages. Furthermore, intracellular trafficking of this receptor was influenced by the nature of the β-glucan ligand, which has significance for the biologic activity of these immunomodulatory carbohydrates. © 2004 by The American Society of Hematology.
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Herre, J., Marshall, A. S. J., Caron, E., Edwards, A. D., Williams, D. L., Schweighoffer, E., … Brown, G. D. (2004). Dectin-1 uses novel mechanisms for yeast phagocytosis in macrophages. Blood, 104(13), 4038–4045. https://doi.org/10.1182/blood-2004-03-1140