Evidence map›Paper›PMID 30107569›Full record

ReviewFEMS microbiology letters2018

Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.

Samuel Wagner, Iwan Grin, Silke Malmsheimer, Nidhi Singh, Claudia E Torres-Vargas, Sibel Westerhausen

Abstract readReview
In one paragraph

Review in FEMS microbiology letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
–field-weighted citation impact
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

100 citing papers in PubMed.

  1. Article
  2. Article
  3. EnterohemorrhagiciScience · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Exploring Mobile Genetic Elements in Vibrio cholerae.Genome biology and evolution · 2025
    Article
  15. Experimental Approaches to Visualize Effector Protein Translocation During Host-Pathogen Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  16. Article
  17. VopX, a novelmBio · 2025
    Article
  18. Review
  19. Article
  20. Review

40 more citing papers are in PubMed but not listed here.

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.

Samuel WagnerUniversity of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany.
Iwan GrinUniversity of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany.
Silke MalmsheimerUniversity of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany.
Nidhi SinghUniversity of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany.
Claudia E Torres-VargasUniversity of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany.
Sibel WesterhausenUniversity of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Virulence-associated type III secretion systems (T3SS) serve the injection of bacterial effector proteins into eukaryotic host cells. They are able to secrete a great diversity of substrate proteins in order to modulate host cell function, and have evolved to sense host cell contact and to inject their substrates through a translocon pore in the host cell membrane. T3SS substrates contain an N-terminal signal sequence and often a chaperone-binding domain for cognate T3SS chaperones. These signals guide the substrates to the machine where substrates are unfolded and handed over to the secretion channel formed by the transmembrane domains of the export apparatus components and by the needle filament. Secretion itself is driven by the proton motive force across the bacterial inner membrane. The needle filament measures 20-150 nm in length and is crowned by a needle tip that mediates host-cell sensing. Secretion through T3SS is a highly regulated process with early, intermediate and late substrates. A strict secretion hierarchy is required to build an injectisome capable of reaching, sensing and penetrating the host cell membrane, before host cell-acting effector proteins are deployed. Here, we review the recent progress on elucidating the assembly, structure and function of T3SS injectisomes.

Indexed as

Bacterial ProteinsCell MembraneEukaryotic CellsType III Secretion SystemsBacterial ProteinsType III Secretion Systems

Identifiers

PMID30107569
PMCPMC6140923

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.