Evidence map›Paper›PMID 23409096›Full record

ArticlePloS one2013

EspO1-2 regulates EspM2-mediated RhoA activity to stabilize formation of focal adhesions in enterohemorrhagic Escherichia coli-infected host cells.

Tomoko Morita-Ishihara, Masashi Miura, Sunao Iyoda, Hidemasa Izumiya, Haruo Watanabe, Makoto Ohnishi, Jun Terajima

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Attaching and effacing pathogens modulate host mitochondrial structure and function.International review of cell and molecular biology · 2023
    Review
  3. Impact of Epithelial Cell Shedding on Intestinal Homeostasis.International journal of molecular sciences · 2022
    Review
  4. Article
  5. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  6. A post-invasion role forThe Journal of biological chemistry · 2020
    Article
  7. Article
  8. Review
  9. Quercetin PreventsFrontiers in microbiology · 2018
    Article
  10. Article
  11. Epithelial cell extrusion: Pathways and pathologies.Seminars in cell & developmental biology · 2017
    Review
  12. Article
  13. 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

7 authors at 2 institutions in 1 country.

Tomoko Morita-IshiharaDepartment of Bacteriology I, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo, Japan. ishihara@nih.go.jp
Masashi Miura
Sunao Iyoda
Hidemasa Izumiya
Haruo Watanabe
Makoto Ohnishi
Jun Terajima
National Institute of Infectious Diseases · JPNagasaki University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enterohemorrhagic Escherichia coli (EHEC) Sakai strain encodes two homologous type III effectors, EspO1-1 and EspO1-2. These EspO1s have amino acid sequence homology with Shigella OspE, which targets integrin-linked kinase to stabilize formation of focal adhesions (FAs). Like OspE, EspO1-1 was localized to FAs in EHEC-infected cells, but EspO1-2 was localized in the cytoplasm. An EHEC ΔespO1-1ΔespO1-2 double mutant induced cell rounding and FA loss in most of infected cells, but neither the ΔespO1-1 nor ΔespO1-2 single mutant did. These results suggested that EspO1-2 functioned in the cytoplasm by a different mechanism from EspO1-1 and OspE. Since several type III effectors modulate Rho GTPase, which contributes to FA formation, we investigated whether EspO1-2 modulates the function of these type III effectors. We identified a direct interaction between EspO1-2 and EspM2, which acts as a RhoA guanine nucleotide exchange factor. Upon ectopic co-expression, EspO1-2 co-localized with EspM2 in the cytoplasm and suppressed EspM2-mediated stress fiber formation. Consistent with these findings, an ΔespO1-1ΔespO1-2ΔespM2 triple mutant did not induce cell rounding in epithelial cells. These results indicated that EspO1-2 interacted with EspM2 to regulate EspM2-mediated RhoA activity and stabilize FA formation during EHEC infection.

Indexed as

ActinsAmino Acid SequenceCell LineCell ShapeCytoplasmEnterohemorrhagic Escherichia coliEscherichia coli ProteinsFocal AdhesionsHost-Pathogen InteractionsHumansMicrofilament ProteinsModels, BiologicalMolecular Sequence DataProtein BindingProtein StabilityProtein TransportActinsEscherichia coli ProteinsespM protein, E coliEspO1-2 protein, E coliMicrofilament ProteinsrhoA GTP-Binding Protein

Identifiers

PMID23409096
PMCPMC3568036
OpenAlexW2094732281

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.