期刊
MOLECULAR IMMUNOLOGY
卷 47, 期 2-3, 页码 575-581出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2009.09.018
关键词
Complement receptor 3; Dectin-1; Zymosan; Respiratory burst
资金
- Landsteiner Foundation
- NIHR Oxford Biomedical Centre
- EU
- Primary Immunodeficiency Association
- Baxter Healthcare
- Jeffrey Modell Foundation
We investigated the role of the beta-glucan receptor, Dectin-1, in the response of human neutrophils to unopsonized Saccharomyces cerevisiae and its major beta-glucan-containing capsular constituent, zymosan. Although reported to be indispensable for yeast phagocytosis in murine phagocytes, human Dectin-1 was not involved in the phagocytosis of S. cerevisiae or zymosan by human neutrophils. Phagocytosis of yeast particles proved to be completely dependent on CD11b/CD18, also known as complement receptor 3 (CR3). The findings were supported by data with neutrophils from a patient suffering from Leukocyte-Adhesion Deficiency type-1 (LAD-1) syndrome lacking CD11b/CD18. In addition, neither the priming by zymosan of the fMLP-induced NADPH-oxidase activity in human neutrophils nor the secretion of IL-8 by human neutrophils in response to zymosan preparations was affected by blocking anti-Dectin-1 antibodies or laminarin as a monovalent inhibitor. As shown by neutrophils from an IRAK-4-deficient patient, the zymosan-induced IL-8 release was also independent of TLR2. In summary, our data show that Dectin-1, although indispensable for recognition of beta-glucan-bearing particles in mice, is not the major receptor for yeast particles in human neutrophils. (C) 2009 Elsevier Ltd. All rights reserved.
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