期刊
ELIFE
卷 7, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.34798
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资金
- Canadian Institutes of Health Research [FDN143202, FDN-154288, PJT-153403, PJT-148548, MOP-86452, MOP-119520]
- Heart and Stroke Foundation of Canada
- National Institutes of Health [AI115947-01, 1R01AI127375-01]
- The Research Training Group 1459
- Natural Sciences and Engineering Research Council of Canada [06261, 477598, 462167]
Candida albicans hyphae can reach enormous lengths, precluding their internalization by phagocytes. Nevertheless, macrophages engulf a portion of the hypha, generating incompletely sealed tubular phagosomes. These frustrated phagosomes are stabilized by a thick cuff of F-actin that polymerizes in response to non-canonical activation of integrins by fungal glycan. Despite their continuity, the surface and invaginating phagosomal membranes retain a strikingly distinct lipid composition. Ptdlns(4,5)P-2 is present at the plasmalemma but is not detectable in the phagosomal membrane, while Ptdlns(3)P and Ptdlns(3,4,5)P-3 co-exist in the phagosomes yet are absent from the surface membrane. Moreover, endo-lysosomal proteins are present only in the phagosomal membrane. Fluorescence recovery after photobleaching revealed the presence of a diffusion barrier that maintains the identity of the open tubular phagosome separate from the plasmalemma. Formation of this barrier depends on Syk, Pyk2/Fak and formin-dependent actin assembly. Antimicrobial mechanisms can thereby be deployed, limiting the growth of the hyphae.
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