H2020 Marie Curie Actions of the European Commission
H2020-MSCA-IF-2016-752022
European Union
European Research Council (ERC)
772853-ENTRAPMENT
European Union
Wellcome Trust
206444/Z/17/Z
European Union
European Research Council (ERC)
679209
European Union
Swiss National Science Foundation
31003A_179255
スイス
引用
ジャーナル: Nat Commun / 年: 2021 タイトル: Mechanistic insight into bacterial entrapment by septin cage reconstitution. 著者: Damián Lobato-Márquez / Jingwei Xu / Gizem Özbaykal Güler / Adaobi Ojiakor / Martin Pilhofer / Serge Mostowy / 要旨: 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 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.