Mechanistic insight into bacterial entrapment by septin cage reconstitution

Damián Lobato-Márquez (), Jingwei Xu, Gizem Özbaykal Güler, Adaobi Ojiakor, Martin Pilhofer and Serge Mostowy ()
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Damián Lobato-Márquez: London School of Hygiene and Tropical Medicine
Jingwei Xu: Eidgenössische Technische Hochschule Zürich
Gizem Özbaykal Güler: London School of Hygiene and Tropical Medicine
Adaobi Ojiakor: London School of Hygiene and Tropical Medicine
Martin Pilhofer: Eidgenössische Technische Hochschule Zürich
Serge Mostowy: London School of Hygiene and Tropical Medicine

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: Abstract Septins are cytoskeletal proteins that assemble into hetero-oligomeric complexes and sense micron-scale membrane curvature. During infection with Shigella flexneri, an invasive enteropathogen, septins restrict actin tail formation by entrapping bacteria in cage-like structures. Here, we reconstitute septin cages in vitro using purified recombinant septin complexes (SEPT2-SEPT6-SEPT7), and study how these recognize bacterial cells and assemble on their surface. We show that septin complexes recognize the pole of growing Shigella cells. An amphipathic helix domain in human SEPT6 enables septins to sense positively curved membranes and entrap bacterial cells. Shigella strains lacking lipopolysaccharide components are more efficiently entrapped in septin cages. Finally, cryo-electron tomography of in vitro cages reveals how septins assemble as filaments on the bacterial cell surface.

Date: 2021
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DOI: 10.1038/s41467-021-24721-5

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