Evidence map›Paper›PMID 34301939›Full record

ArticleNature communications2021

Mechanistic insight into bacterial entrapment by septin cage reconstitution.

Damián Lobato-Márquez, Jingwei Xu, Gizem Özbaykal Güler, Adaobi Ojiakor, Martin Pilhofer, Serge Mostowy

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.1field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Proximity biotinylation at the host-bioRxiv : the preprint server for biology · 2025
    Article
  8. Review
  9. Article
  10. The Evolutionary Origins and Ancestral Features of Septins.bioRxiv : the preprint server for biology · 2024
    Article
  11. Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024
    Article
  12. The evolutionary origins and ancestral features of septins.Frontiers in cell and developmental biology · 2024
    Article
  13. Article
  14. Science advances · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Curvature sensing as an emergent property of multiscale assembly of septins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Damián Lobato-MárquezDepartment of Infection Biology, London School of Hygiene and Tropical Medicine, London, UK. damian.marquez@lshtm.ac.uk.ORCID 0000-0002-0044-7588
Jingwei XuDepartment of Biology, Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zürich, Zürich, Switzerland.ORCID 0000-0003-1833-1513
Gizem Özbaykal GülerDepartment of Infection Biology, London School of Hygiene and Tropical Medicine, London, UK.
Adaobi OjiakorDepartment of Infection Biology, London School of Hygiene and Tropical Medicine, London, UK.
Martin PilhoferDepartment of Biology, Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zürich, Zürich, Switzerland.
Serge MostowyDepartment of Infection Biology, London School of Hygiene and Tropical Medicine, London, UK. serge.mostowy@lshtm.ac.uk.ORCID 0000-0002-7286-6503
London School of Hygiene & Tropical Medicine · GBETH Zurich · CH

Funding

Wellcome TrustWellcome Trust 206444/Z/17/Z
6 · The paper itself

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.

Indexed as

ActinsBacterial ProteinsCell MembraneDNA-Binding ProteinsDysentery, BacillaryGreen Fluorescent ProteinsHeLa CellsHumansLipopolysaccharidesMicroscopy, FluorescenceMutationProtein BindingRecombinant ProteinsSeptinsShigella flexneriTranscription FactorsActinsBacterial ProteinsDNA-Binding ProteinsGreen Fluorescent ProteinsLipopolysaccharidesRecombinant ProteinsSEPTIN6 protein, humanSeptinsTranscription FactorsvirG protein, Shigella flexneri

Identifiers

PMID34301939
PMCPMC8302635
OpenAlexW3183264657

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.