Integrin-based diffusion barrier separates membrane domains enabling the formation of microbiostatic frustrated phagosomes.

Abstract:

: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. PtdIns(4,5)P2 is present at the plasmalemma but is not detectable in the phagosomal membrane, while PtdIns(3)P and PtdIns(3,4,5)P3 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.

journal_name

Elife

journal_title

eLife

authors

Maxson ME,Naj X,O'Meara TR,Plumb JD,Cowen LE,Grinstein S

doi

10.7554/eLife.34798

subject

Has Abstract

pub_date

2018-03-19 00:00:00

issn

2050-084X

pii

34798

journal_volume

7

pub_type

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