Evidence map›Paper›PMID 21187904›Full record

ArticlePLoS pathogens2010

NleC, a type III secretion protease, compromises NF-κB activation by targeting p65/RelA.

Hilo Yen, Tadasuke Ooka, Atsushi Iguchi, Tetsuya Hayashi, Nakaba Sugimoto, Toru Tobe

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

88 citing papers in PubMed, 162 citations in OpenAlex.

  1. Article
  2. Article
  3. Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026
    Article
  4. EnteropathogeniceLife · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. AIP56, an AB toxin secreted byFrontiers in immunology · 2024
    Article
  11. Article
  12. Review
  13. Speaking the host language: howMicrobiology (Reading, England) · 2023
    Review
  14. Review
  15. Review
  16. Pathophysiology of enteropathogenicJournal of veterinary science · 2022
    Review
  17. Bacterial Toxin and Effector Regulation of Intestinal Immune Signaling.Frontiers in cell and developmental biology · 2022
    Review
  18. Review
  19. Article
  20. The T3SS Effector Protease NleC Is Active withinPathogens (Basel, Switzerland) · 2021
    Article

28 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 at 2 institutions in 1 country.

Hilo YenDepartment of Microbiology and Immunology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Tadasuke Ooka
Atsushi Iguchi
Tetsuya Hayashi
Nakaba Sugimoto
Toru Tobe
Osaka University · JPUniversity of Miyazaki · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The NF-κB signaling pathway is central to the innate and adaptive immune responses. Upon their detection of pathogen-associated molecular patterns, Toll-like receptors on the cell surface initiate signal transduction and activate the NF-κB pathway, leading to the production of a wide array of inflammatory cytokines, in attempt to eradicate the invaders. As a countermeasure, pathogens have evolved ways to subvert and manipulate this system to their advantage. Enteropathogenic and enterohemorrhagic Escherichia coli (EPEC and EHEC) are closely related bacteria responsible for major food-borne diseases worldwide. Via a needle-like protein complex called the type three secretion system (T3SS), these pathogens deliver virulence factors directly to host cells and modify cellular functions, including by suppressing the inflammatory response. Using gain- and loss-of-function screenings, we identified two bacterial effectors, NleC and NleE, that down-regulate the NF-κB signal upon being injected into a host cell via the T3SS. A recent report showed that NleE inhibits NF-κB activation, although an NleE-deficient pathogen was still immune-suppressive, indicating that other anti-inflammatory effectors are involved. In agreement, our present results showed that NleC was also required to inhibit inflammation. We found that NleC is a zinc protease that disrupts NF-κB activation by the direct cleavage of NF-κB's p65 subunit in the cytoplasm, thereby decreasing the available p65 and reducing the total nuclear entry of active p65. More importantly, we showed that a mutant EPEC/EHEC lacking both NleC and NleE (ΔnleC ΔnleE) caused greater inflammatory response than bacteria carrying ΔnleC or ΔnleE alone. This effect was similar to that of a T3SS-defective mutant. In conclusion, we found that NleC is an anti-inflammatory bacterial zinc protease, and that the cooperative function of NleE and NleC disrupts the NF-κB pathway and accounts for most of the immune suppression caused by EHEC/EPEC.

Indexed as

Immune EvasionEnterohemorrhagic Escherichia coliEnteropathogenic Escherichia coliEscherichia coli ProteinsNF-kappa BPeptide HydrolasesTranscription Factor RelAVirulence FactorsEscherichia coli ProteinsNF-kappa BNleE protein, E coliPeptide HydrolasesTranscription Factor RelAVirulence FactorsZ0986 protein, E coli

Identifiers

PMID21187904
PMCPMC3002990
OpenAlexW2005943324

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.