Evidence map›Paper›PMID 21498649›Full record

ArticleJournal of bacteriology2011

Interactions and predicted host membrane topology of the enteropathogenic Escherichia coli translocator protein EspB.

Wensheng Luo, Michael S Donnenberg

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

  1. ThemSphere · 2024
    Article
  2. Article
  3. Article
  4. Assay for Type III Secretion in Escherichia coli.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  5. Article
  6. Review
  7. Cryoelectron-microscopy structure of the enteropathogenicProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016
    Review
  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

2 authors at 1 institution in 1 country.

Wensheng LuoDivision of Infectious Diseases, Department of Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Michael S Donnenberg
University of Maryland, Baltimore · US

Funding

The eae Gene Cluster of Enteropathogenic E.coliR01AI032074 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI DONNENBERG, MICHAEL S · 1997 to 2012
$3.7M
The eae Gene Cluster of Enteropathogenic E.coliR56AI032074 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI DONNENBERG, MICHAEL S · 2007 to 2007
$375k
EAE GENE CLUSTER OF ENTEROPATHOGENIC E. COLIR29AI032074 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI DONNENBERG, MICHAEL S · 1992 to 1996
–
NIAID NIH HHS AI32074NIAID NIH HHS R01 AI032074NIAID NIH HHS R56 AI032074
6 · The paper itself

Abstract

Type 3 secretion systems (T3SSs) are critical for the virulence of numerous deadly Gram-negative pathogens. T3SS translocator proteins are required for effector proteins to traverse the host cell membrane and perturb cell function. Translocator proteins include two hydrophobic proteins, represented in enteropathogenic Escherichia coli (EPEC) by EspB and EspD, which are thought to interact and form a pore in the host membrane. Here we adapted a sequence motif recognized by a host kinase to demonstrate that residues on the carboxyl-terminal side of the EspB transmembrane domain are localized to the host cell cytoplasm. Using functional internal polyhistidine tags, we confirm an interaction between EspD and EspB, and we demonstrate, for the first time, an interaction between EspD and the hydrophilic translocator protein EspA. Using a panel of espB insertion mutations, we describe two regions on either side of a putative transmembrane domain that are required for the binding of EspB to EspD. Finally, we demonstrate that EspB variants incapable of binding EspD fail to adopt the proper host cell membrane topology. These results provide new insights into interactions between translocator proteins critical for virulence.

Indexed as

Bacterial Outer Membrane ProteinsCell MembraneEnteropathogenic Escherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialHeLa CellsHumansMutationPhosphotransferasesProtein BindingProtein Structure, TertiaryBacterial Outer Membrane ProteinsEaeB protein, E coliEscherichia coli ProteinsEspA protein, E coliEspD protein, E coliPhosphotransferases

Identifiers

PMID21498649
PMCPMC3133209
OpenAlexW1964490261

What OpenQuestion holds

Textmetadata
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.