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Review
. 2018 Sep 3;9(5):365-374.
doi: 10.1080/21541248.2016.1240494. Epub 2016 Nov 1.

Diverted recycling-Shigella subversion of Rabs

Noelia López-Montero  1 , Jost Enninga  1
Affiliations
Review

Diverted recycling-Shigella subversion of Rabs

Noelia López-Montero et al. Small GTPases. .

Abstract

Small GTPases of the Rab protein family control intracellular vesicular trafficking to allow their communication and maintenance. It is a common strategy for intracellular bacteria to exploit these pathways to shape their respective niches for survival. The subversion of Rabs for the generation of an intracellular environment favoring the pathogen has been described almost exclusively for intracellular bacteria that reside within bacterial containing vacuoles (BCVs). However, less is known about Rab subversion for bacteria that rupture the BCV to reach the host cytoplasm. Here, we provide recent examples of Rab targeting by both groups of intracellular bacteria with a special focus on Shigella, the causative agent of bacillary dysentery. Shigella recruits Rab11, the hallmark of the perinuclear recycling compartment to in situ formed macropinosomes at the entry foci via the bacterial effector IpgD. This leads to efficient BCV rupture and cytosolic escape. We discuss the concept of diverted recycling through host Rab GTPases that emerges as a novel pathogen strategy.

Keywords: Rab subversion; Rab11; Shigella flexneri; bacterial containing vacuole; intracellular bacteria; macropinocytosis; vacuolar rupture; vesicular traffic.

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Figures

Figure 1.
Figure 1.
Schematic representation of macropinosome-like vesicles induced by Shigella infection in comparison to the canonical macropinocytic pathway. On the right side, canonical macropinosomes traffic along the endolysosomal pathway, where they are eventually degraded. Rab5 (red) is first recruited to nascent macropinosomes, similar to its recruitment to early endosomes. Then, it is replaced by Rab7 (green). Acquisition of Rab7 implies retrograde transport along microtubules and subsequent fusion with lysosomes. Upon fusion with lysosomes, macropinosomes acquire lysosomal markers such as Lamp1 and hydrolytic enzymes leading to their acidification. In contrast, macropinosome-like vesicles induced by Shigella infection block their maturation before their fusion with lysosomes (left side). Rab11 (magenta) is instead recruited by the bacterial effector IpgD. Bacterial subversion of Rab11, and its recruitment to Shigella-induced macropinosomes, promotes efficient vacuolar escape. ES, extracellular space; C, cytosol; MC, macropinocytic cup; SIM, Shigella induced macropinosome; BCV, bacteria containing vacuole; B, bacteria; EM, early macropinosome; LM, late macropinosome; LM/Ly, late macropinosome-lysosome; Ly, lysosome; arrow, intramacropinosomal vesicle.
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This work was supported by the LabEx consortium IBEID, and by the Institut Pasteur CARNOT-MIE program. J.E also acknowledges support of an ERC starting grant (Rupteffects, Nr. 261166).

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