Evidence map›Paper›PMID 32092125›Full record

ArticlePLoS pathogens2020

Cryo-EM structure of the Shigella type III needle complex.

Michele Lunelli, Antje Kamprad, Jörg Bürger, Thorsten Mielke, Christian M T Spahn, Michael Kolbe

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

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  3. Molecular basis for curvature formation in SepF polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  9. Differential regulation ofFrontiers in cellular and infection microbiology · 2023
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  14. Helical reconstruction ofBiochemistry and biophysics reports · 2021
    Article
  15. Review
  16. Article
  17. Article
  18. TheMicroorganisms · 2021
    Review
  19. Interesting Biochemistries in the Structure and Function of Bacterial Effectors.Frontiers in cellular and infection microbiology · 2021
    Review
  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

6 authors at 4 institutions in 1 country.

Michele LunelliDepartment of Structural Infection Biology, Centre for Structural Systems Biology (CSSB), Helmholtz-Centre for Infection Research (HZI), Hamburg, Germany.ORCID 0000-0002-4956-3096
Antje KampradDepartment of Structural Infection Biology, Centre for Structural Systems Biology (CSSB), Helmholtz-Centre for Infection Research (HZI), Hamburg, Germany.
Jörg BürgerInstitute for Medical Physics and Biophysics, Charité Universitätsmedizin Berlin, Berlin, Germany.ORCID 0000-0002-4326-5047
Thorsten MielkeMax Planck Institute for Molecular Genetics, Berlin, Germany.ORCID 0000-0001-9275-3146
Christian M T SpahnInstitute for Medical Physics and Biophysics, Charité Universitätsmedizin Berlin, Berlin, Germany.
Michael KolbeDepartment of Structural Infection Biology, Centre for Structural Systems Biology (CSSB), Helmholtz-Centre for Infection Research (HZI), Hamburg, Germany.ORCID 0000-0002-1219-0249
Charité - Universitätsmedizin Berlin · DEMax Planck Institute for Infection Biology · DEMax Planck Institute for Molecular Genetics · DEUniversität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Type III Secretion Systems (T3SS) needle complex is a conserved syringe-shaped protein translocation nanomachine with a mass of about 3.5 MDa essential for the survival and virulence of many Gram-negative bacterial pathogens. This system is composed of a membrane-embedded basal body and an extracellular needle that deliver effector proteins into host cells. High-resolution structures of the T3SS from different organisms and infection stages are needed to understand the underlying molecular mechanisms of effector translocation. Here, we present the cryo-electron microscopy structure of the isolated Shigella T3SS needle complex. The inner membrane (IM) region of the basal body adopts 24-fold rotational symmetry and forms a channel system that connects the bacterial periplasm with the export apparatus cage. The secretin oligomer adopts a heterogeneous architecture with 16- and 15-fold cyclic symmetry in the periplasmic N-terminal connector and C-terminal outer membrane ring, respectively. Two out of three IM subunits bind the secretin connector via a β-sheet augmentation. The cryo-EM map also reveals the helical architecture of the export apparatus core, the inner rod, the needle and their intervening interfaces.

Indexed as

Cryoelectron MicroscopyBacterial ProteinsCell MembraneProtein Conformation, beta-StrandProtein DomainsShigellaType III Secretion SystemsBacterial ProteinsType III Secretion Systems

Identifiers

PMID32092125
PMCPMC7058355
OpenAlexW3008351451

What OpenQuestion holds

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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.