Actin and phosphoinositide recruitment to fully formed Candida albicans phagosomes in mouse macrophages

Sigrid E M Heinsbroek, Lynn A Kamen, Philip R Taylor, Gordon D Brown, Joel Swanson, Siamon Gordon

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12 Citations (Scopus)

Abstract

Candida albicans is a dimorphic yeast that enters macrophages (Mφ) via the β-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 Mφ. 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)P2, PI(3,4,5)P3, PI(3,4)P2, 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 Mφ.
Original languageEnglish
Pages (from-to)244-253
Number of pages10
JournalJournal of Innate Immunity
Volume1
Issue number3
Early online date12 Nov 2008
DOIs
Publication statusPublished - Apr 2009

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Keywords

  • life imaging
  • macrophages
  • phagocytosis
  • candida albicans
  • phosphoinositides
  • yeast

Cite this

Heinsbroek, S. E. M., Kamen, L. A., Taylor, P. R., Brown, G. D., Swanson, J., & Gordon, S. (2009). Actin and phosphoinositide recruitment to fully formed Candida albicans phagosomes in mouse macrophages. Journal of Innate Immunity, 1(3), 244-253. https://doi.org/10.1159/000173694