Complement receptor 3, not Dectin-1, is the major receptor on human neutrophils for beta-glucan-bearing particles.
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 De...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2009
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| _version_ | 1797086992506290176 |
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| author | van Bruggen, R Drewniak, A Jansen, M van Houdt, M Roos, D Chapel, H Verhoeven, A Kuijpers, T |
| author_facet | van Bruggen, R Drewniak, A Jansen, M van Houdt, M Roos, D Chapel, H Verhoeven, A Kuijpers, T |
| author_sort | van Bruggen, R |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T02:29:47Z |
| format | Journal article |
| id | oxford-uuid:a6d99653-6aeb-43c7-9d88-f8cfe65bcc16 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:29:47Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:a6d99653-6aeb-43c7-9d88-f8cfe65bcc162022-03-27T02:50:17ZComplement receptor 3, not Dectin-1, is the major receptor on human neutrophils for beta-glucan-bearing particles.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a6d99653-6aeb-43c7-9d88-f8cfe65bcc16EnglishSymplectic Elements at Oxford2009van Bruggen, RDrewniak, AJansen, Mvan Houdt, MRoos, DChapel, HVerhoeven, AKuijpers, TWe 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. |
| spellingShingle | van Bruggen, R Drewniak, A Jansen, M van Houdt, M Roos, D Chapel, H Verhoeven, A Kuijpers, T Complement receptor 3, not Dectin-1, is the major receptor on human neutrophils for beta-glucan-bearing particles. |
| title | Complement receptor 3, not Dectin-1, is the major receptor on human neutrophils for beta-glucan-bearing particles. |
| title_full | Complement receptor 3, not Dectin-1, is the major receptor on human neutrophils for beta-glucan-bearing particles. |
| title_fullStr | Complement receptor 3, not Dectin-1, is the major receptor on human neutrophils for beta-glucan-bearing particles. |
| title_full_unstemmed | Complement receptor 3, not Dectin-1, is the major receptor on human neutrophils for beta-glucan-bearing particles. |
| title_short | Complement receptor 3, not Dectin-1, is the major receptor on human neutrophils for beta-glucan-bearing particles. |
| title_sort | complement receptor 3 not dectin 1 is the major receptor on human neutrophils for beta glucan bearing particles |
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