Cell Host & Microbe
Volume 24, Issue 6, 12 December 2018, Pages 866-874.e4
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Short Article
Septins Recognize and Entrap Dividing Bacterial Cells for Delivery to Lysosomes

https://doi.org/10.1016/j.chom.2018.11.005Get rights and content
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Highlights

  • Septins are recruited to micron-scale curvature of dividing intracellular bacteria

  • Cardiolipin promotes the recruitment of septins to curved bacterial membranes

  • Following recruitment, septins assemble into cages around growing bacterial cells

  • Septins inhibit bacterial division via recruitment of autophagic and lysosomal machinery

Summary

The cytoskeleton occupies a central role in cellular immunity by promoting bacterial sensing and antibacterial functions. Septins are cytoskeletal proteins implicated in various cellular processes, including cell division. Septins also assemble into cage-like structures that entrap cytosolic Shigella, yet how septins recognize bacteria is poorly understood. Here, we discover that septins are recruited to regions of micron-scale membrane curvature upon invasion and division by a variety of bacterial species. Cardiolipin, a curvature-specific phospholipid, promotes septin recruitment to highly curved membranes of Shigella, and bacterial mutants lacking cardiolipin exhibit less septin cage entrapment. Chemically inhibiting cell separation to prolong membrane curvature or reducing Shigella cell growth respectively increases and decreases septin cage formation. Once formed, septin cages inhibit Shigella cell division upon recruitment of autophagic and lysosomal machinery. Thus, recognition of dividing bacterial cells by the septin cytoskeleton is a powerful mechanism to restrict the proliferation of intracellular bacterial pathogens.

Keywords

cardiolipin
cytoskeleton
FtsZ
membrane curvature
septins
Shigella

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