Evidence map›Paper›PMID 19165331›Full record

ArticlePLoS pathogens2009

The IpaC carboxyterminal effector domain mediates Src-dependent actin polymerization during Shigella invasion of epithelial cells.

Joëlle Mounier, Michel R Popoff, Jost Enninga, Margaret C Frame, Philippe J Sansonetti, Guy Tran Van Nhieu

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.6field-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

59 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Review
  3. RACK1 promotesiScience · 2023
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. The T3SS ofMicroorganisms · 2020
    Review
  14. Article
  15. Article
  16. The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019
    Review
  17. Taming the Triskelion: Bacterial Manipulation of Clathrin.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  18. Article
  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

6 authors at 3 institutions in 2 countries.

Joëlle MounierUnité de Pathogénie Microbienne Moléculaire, Institut Pasteur, Paris, France.
Michel R Popoff
Jost Enninga
Margaret C Frame
Philippe J Sansonetti
Guy Tran Van Nhieu
Institut Pasteur · FRInserm · FRWestern General Hospital · GB

Funding

Pathogen-host Interactions that Remodel the CytoskeletonR01AI067949 · NIAID · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI IZARD, TINA · 2006 to 2010
$2.0M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI067949
6 · The paper itself

Abstract

Shigella, the causative agent of bacillary dysentery, invades epithelial cells by locally reorganizing the actin cytoskeleton. Shigella invasion requires actin polymerization dependent on the Src tyrosine kinase and a functional bacterial type III secretion (T3S) apparatus. Using dynamic as well as immunofluorescence microscopy, we show that the T3S translocon component IpaC allows the recruitment of the Src kinase required for actin polymerization at bacterial entry sites during the initial stages of Shigella entry. Src recruitment occurred at bacterial-cell contact sites independent of actin polymerization at the onset of the invasive process and was still observed in Shigella strains mutated for translocated T3S effectors of invasion. A Shigella strain with a polar mutation that expressed low levels of the translocator components IpaB and IpaC was fully proficient for Src recruitment and bacterial invasion. In contrast, a Shigella strain mutated in the IpaC carboxyterminal effector domain that was proficient for T3S effector translocation did not induce Src recruitment. Consistent with a direct role for IpaC in Src activation, cell incubation with the IpaC last 72 carboxyterminal residues fused to the Iota toxin Ia (IaC) component that translocates into the cell cytosol upon binding to the Ib component led to Src-dependent ruffle formation. Strikingly, IaC also induced actin structures resembling bacterial entry foci that were enriched in activated Src and were inhibited by the Src inhibitor PP2. These results indicate that the IpaC effector domain determines Src-dependent actin polymerization and ruffle formation during bacterial invasion.

Indexed as

ActinsAnimalsAntigens, BacterialBridged Bicyclo Compounds, HeterocyclicHeLa CellsHemolysisHorsesHumansPlasmidsProtein Structure, Tertiaryrac1 GTP-Binding ProteinShigella flexnerisrc-Family KinasesThiazolidinesActinsAntigens, BacterialBridged Bicyclo Compounds, HeterocyclicIpaC protein, ShigellaIpgB1 protein, Shigella flexnerilatrunculin Brac1 GTP-Binding Proteinsrc-Family KinasesThiazolidines

Identifiers

PMID19165331
PMCPMC2621354
OpenAlexW2151889957

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.