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dc.contributor.author
Lobato-Márquez, Damián
dc.contributor.author
Xu, Jingwei
dc.contributor.author
Özbaykal Güler, Gizem
dc.contributor.author
Ojiakor, Adaobi
dc.contributor.author
Pilhofer, Martin
dc.contributor.author
Mostowy, Serge
dc.date.accessioned
2021-08-05T06:20:47Z
dc.date.available
2021-08-05T03:16:26Z
dc.date.available
2021-08-05T06:20:47Z
dc.date.issued
2021-07-23
dc.identifier.issn
2041-1723
dc.identifier.other
10.1038/s41467-021-24721-5
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/499581
dc.identifier.doi
10.3929/ethz-b-000499581
dc.description.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.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Nature Publishing Group
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
Bacterial host response
en_US
dc.subject
Cellular microbiology
en_US
dc.subject
Cytoskeleton
en_US
dc.subject
Pathogens
en_US
dc.title
Mechanistic insight into bacterial entrapment by septin cage reconstitution
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
Nature Communications
ethz.journal.volume
12
en_US
ethz.journal.issue
1
en_US
ethz.journal.abbreviated
Nat Commun
ethz.pages.start
4511
en_US
ethz.size
14 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.grant
Structure, function, and evolution of bacterial contractile injection systems
en_US
ethz.grant
Multiscale model of bacterial cell-cell interactions
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::09463 - Pilhofer, Martin / Pilhofer, Martin
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::09463 - Pilhofer, Martin / Pilhofer, Martin
ethz.grant.agreementno
179255
ethz.grant.agreementno
679209
ethz.grant.fundername
SNF
ethz.grant.fundername
EC
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.funderDoi
10.13039/501100000780
ethz.grant.program
H2020
ethz.grant.program
Projekte Lebenswissenschaften
ethz.date.deposited
2021-08-05T03:16:29Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2021-08-05T06:20:53Z
ethz.rosetta.lastUpdated
2022-03-29T10:56:26Z
ethz.rosetta.versionExported
true
ethz.COinS
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