Evidence map›Paper›PMID 21541301›Full record

ArticlePloS one2011

The EHEC type III effector NleL is an E3 ubiquitin ligase that modulates pedestal formation.

Heather Piscatelli, Shalaka A Kotkar, Megan E McBee, Sureshkumar Muthupalani, David B Schauer, Robert E Mandrell, John M Leong, Daoguo Zhou

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Bacteria and Allergic Diseases.International journal of molecular sciences · 2024
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Bacterial mimicry of eukaryotic HECT ubiquitin ligation.bioRxiv : the preprint server for biology · 2023
    Article
  10. Speaking the host language: howMicrobiology (Reading, England) · 2023
    Review
  11. Article
  12. Article
  13. Interesting Biochemistries in the Structure and Function of Bacterial Effectors.Frontiers in cellular and infection microbiology · 2021
    Review
  14. Review
  15. Review
  16. Review
  17. Functional diversification of the NleG effector family in enterohemorrhagicProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. Article
  20. 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

8 authors at 4 institutions in 1 country.

Heather PiscatelliDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana, United States of America.
Shalaka A Kotkar
Megan E McBee
Sureshkumar Muthupalani
David B Schauer
Robert E Mandrell
John M Leong
Daoguo Zhou
Massachusetts Institute of Technology · USPurdue University West Lafayette · USUnited States Department of Agriculture · USUniversity of Massachusetts Chan Medical School · US

Funding

Role of E3 ubiquitin ligase in Salmonella-induced inflammationK02AI068655 · NIAID · PURDUE UNIVERSITY · PI ZHOU, DAOGUO · 2007 to 2011
$552k
Salmonella SopA is a functional mimicry of eukaryotic E3 protein ubiquitin ligaseR21AI078092 · NIAID · PURDUE UNIVERSITY · PI ZHOU, DAOGUO · 2009 to 2010
$419k
NIAID NIH HHS AI068655NIAID NIH HHS AI078092NIAID NIH HHS K02 AI068655NIAID NIH HHS R21 AI078092
6 · The paper itself

Abstract

Enterohemorrhagic Escherichia coli (EHEC) O157:H7 causes hemorrhagic colitis and may result in potentially fatal hemolytic uremia syndrome in humans. EHEC colonize the intestinal mucosa and promote the formation of actin-rich pedestals via translocated type III effectors. Two EHEC type III secreted effectors, Tir and EspFu/TccP, are key players for pedestal formation. We discovered that an EHEC effector protein called Non-LEE-encoded Ligase (NleL) is an E3 ubiquitin ligase. In vitro, we showed that the NleL C753 residue is critical for its E3 ligase activity. Functionally, we demonstrated that NleL E3 ubiquitin ligase activity is involved in modulating Tir-mediated pedestal formation. Surprisingly, EHEC mutant strain deficient in the E3 ligase activity induced more pedestals than the wild-type strain. The canonical EPEC strain E2348/69 normally lacks the nleL gene, and the ectopic expression of the wild-type EHEC nleL, but not the catalytically-deficient nleL(C753A) mutant, in this strain resulted in fewer actin-rich pedestals. Furthermore, we showed that the C. rodentium NleL homolog is a E3 ubiquitin ligase and is required for efficient infection of murine colonic epithelial cells in vivo. In summary, our study demonstrated that EHEC utilizes NleL E3 ubiquitin ligase activity to modulate Tir-mediated pedestal formation.

Indexed as

AnimalsCell Surface ExtensionsCitrobacter rodentiumDown-RegulationEscherichia coli O157Escherichia coli ProteinsHeLa CellsHumansMiceMice, Inbred C57BLMutant ProteinsProtein TransportRecombinant Fusion ProteinsUbiquitinationUbiquitin-Protein LigasesVirulenceEscherichia coli ProteinsMutant ProteinsNleL protein, E coliRecombinant Fusion ProteinsUbiquitin-Protein Ligases

Identifiers

PMID21541301
PMCPMC3082576
OpenAlexW2096787468

What OpenQuestion holds

Textmetadata
LicenceCC0
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.