期刊
JOURNAL OF IMMUNOLOGY
卷 196, 期 5, 页码 2249-2261出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1401545
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资金
- National Institutes of Health [5R01 A1 092084, 1R01 A1 097519]
- National Institutes of Health/National Institute of Allergy and Infectious Diseases [1K08AI110655, T32 A1007061-35, KL2 TR001100]
Dectin-1 and TLR9 play distinct roles in the recognition and induction of innate immune responses to Aspergillus fumigatus and Candida albicans. Dectin-1 is a receptor for the major fungal cell wall carbohydrate beta-1,3 glucan that induces inflammatory cytokines and controls phagosomal maturation through spleen tyrosine kinase activation. TLR9 is an endosomal TLR that also modulates the inflammatory cytokine response to fungal pathogens. In this study, we demonstrate that beta-1,3 glucan beads are sufficient to induce dynamic redistribution and accumulation of cleaved TLR9 to phagosomes. Trafficking of TLR9 to A. fumigatus and C. albicans phagosomes requires Dectin-1 recognition. Inhibition of phagosomal acidification blocks TLR9 accumulation on phagosomes containing beta-1,3 glucan beads. Dectin-1-mediated spleen tyrosine kinase activation is required for TLR9 trafficking to beta-1,3 glucan-, A. fumigatus-, and C. albicans-containing phagosomes. In addition, Dectin-1 regulates TLR9-dependent gene expression. Collectively, our study demonstrates that recognition of beta-1,3 glucan by Dectin-1 triggers TLR9 trafficking to beta-1,3 glucan-containing phagosomes, which may be critical in coordinating innate antifungal defense.
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