
Open access
Author
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Date
2021-07-23Type
- Journal Article
Citations
Cited 10 times in
Web of Science
Cited 11 times in
Scopus
ETH Bibliography
yes
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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. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000499581Publication status
publishedExternal links
Journal / series
Nature CommunicationsVolume
Pages / Article No.
Publisher
Nature Publishing GroupSubject
Bacterial host response; Cellular microbiology; Cytoskeleton; PathogensOrganisational unit
09463 - Pilhofer, Martin / Pilhofer, Martin
Funding
179255 - Structure, function, and evolution of bacterial contractile injection systems (SNF)
679209 - Multiscale model of bacterial cell-cell interactions (EC)
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Show all metadata
Citations
Cited 10 times in
Web of Science
Cited 11 times in
Scopus
ETH Bibliography
yes
Altmetrics