Evidence map›Paper›PMID 25353930›Full record

ArticleMolecular microbiology2015

Three-dimensional electron microscopy reconstruction and cysteine-mediated crosslinking provide a model of the type III secretion system needle tip complex.

Martin Cheung, Da-Kang Shen, Fumiaki Makino, Takayuki Kato, A Dorothea Roehrich, Isabel Martinez-Argudo, Matthew L Walker, Isabel Murillo, Xia Liu, Maria Pain and 8 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 48 citations in OpenAlex.

  1. Multifunctional antibody responses from a primateScience translational medicine · 2026
    Article
  2. Review
  3. Review
  4. Review
  5. Cryo-EM of the injectisome and type III secretion systems.Current opinion in structural biology · 2022
    Review
  6. Cryo-EM structure of the needle filament tip complex of theProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. TheMicroorganisms · 2021
    Review
  9. Structural Insights ofFrontiers in cellular and infection microbiology · 2021
    Article
  10. The T3SS ofMicroorganisms · 2020
    Review
  11. Review
  12. Article
  13. Article
  14. The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019
    Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article
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

18 authors at 4 institutions in 3 countries.

Martin CheungSchools of Cellular & Molecular Medicine and Biochemistry, University of Bristol, Bristol, BS8 1TD, UK.
Da-Kang Shen
Fumiaki Makino
Takayuki Kato
A Dorothea Roehrich
Isabel Martinez-Argudo
Matthew L Walker
Isabel Murillo
Xia Liu
Maria Pain
James Brown
Gordon Frazer
Judith Mantell
Petros Mina
Thomas Todd
Richard B Sessions
Keiichi Namba
Ariel J Blocker
University of Bristol · GBOsaka University · JPCornwall Council · GBUbe Frontier University · JP

Funding

Medical Research Council G0701243Medical Research Council MRJ002097Medical Research Council MR/J002097/1Wellcome Trust 082398Wellcome Trust 088231Wellcome Trust 104634
6 · The paper itself

Abstract

Type III secretion systems are found in many Gram-negative bacteria. They are activated by contact with eukaryotic cells and inject virulence proteins inside them. Host cell detection requires a protein complex located at the tip of the device's external injection needle. The Shigella tip complex (TC) is composed of IpaD, a hydrophilic protein, and IpaB, a hydrophobic protein, which later forms part of the injection pore in the host membrane. Here we used labelling and crosslinking methods to show that TCs from a ΔipaB strain contain five IpaD subunits while the TCs from wild-type can also contain one IpaB and four IpaD subunits. Electron microscopy followed by single particle and helical image analysis was used to reconstruct three-dimensional images of TCs at ∼ 20 Å resolution. Docking of an IpaD crystal structure, constrained by the crosslinks observed, reveals that TC organisation is different from that of all previously proposed models. Our findings suggest new mechanisms for TC assembly and function. The TC is the only site within these secretion systems targeted by disease-protecting antibodies. By suggesting how these act, our work will allow improvement of prophylactic and therapeutic strategies.

Indexed as

Bacterial Secretion SystemsAntigens, BacterialBacterial ProteinsCross-Linking ReagentsCysteineImaging, Three-DimensionalMicroscopy, ElectronModels, MolecularMolecular Docking SimulationProtein MultimerizationProtein Structure, SecondaryShigella flexneriAntigens, BacterialBacterial ProteinsBacterial Secretion SystemsCross-Linking ReagentsCysteineipaB protein, ShigellaIpaD protein, Shigella flexneri

Identifiers

PMID25353930
PMCPMC4539596
OpenAlexW2157959557

What OpenQuestion 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 OpenQuestion graph.