Journal
JOURNAL OF INNATE IMMUNITY
Volume 1, Issue 3, Pages 244-253Publisher
KARGER
DOI: 10.1159/000173694
Keywords
Life imaging; Macrophages; Phagocytosis; Candida albicans; Phosphoinositides; Yeast
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Funding
- NIH [AI35950, AI64668]
- Wellcome Trust
- Medical Research Council UK
- EPA Cephalosporin Scholarship
- Henry Goodger Scholarship
- Wellcome Trust International Senior Research Fellow in Biomedical Science in South Africa
- Wellcome Trust Research Career Development Fellow [070579]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R21AI035950, R01AI035950, R01AI064668] Funding Source: NIH RePORTER
- MRC [G0601617, G0500623] Funding Source: UKRI
- Medical Research Council [G0601617, G0500623] Funding Source: researchfish
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Candida albicans is a dimorphic yeast that enters macrophages (M phi) via the beta-glucan receptor dectin-1. Phagocytosis of C. albicans is characterized by actin polymerization, Syk kinase activation and rapid acquisition of phagolysosomal markers. In mice, C. albicans are able to resist the harsh environment of the phagosome and form pseudohyphae inside the phagolysosomal compartment, eventually extending from the M phi. In this study, we investigated these unique C. albicans phagosomes and found that actin localized dynamically around the phagosomes, before disintegrating. Membrane phosphoinositides, PI(4,5)P-2, PI(3,4,5)P-3, PI(3,4)P-2, and PI(3)P also localized to the phagosomes. Localization was not related to actin polymerization, and inhibitor studies showed that polymerization of actin on the C. albicans phagosome was independent of PI3K. The ability of mature C. albicans phagosomes to stimulate actin polymerization could facilitate the escape of the growing yeast from the M phi. Copyright (C) 2008 S. Karger AG, Basel
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