Evidence map›Paper›PMID 20971903›Full record

ArticleJournal of bacteriology2011

Assembly of the type II secretion system: identification of ExeA residues critical for peptidoglycan binding and secretin multimerization.

Gang Li, Alicia Miller, Harold Bull, S Peter Howard

Abstract 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Peptidoglycan deacetylation controls type IV secretion and the intracellular survival of the bacterial pathogenProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Article
  4. Article
  5. Review
  6. Interplay between Peptidoglycan Biology and Virulence in Gram-Negative Pathogens.Microbiology and molecular biology reviews : MMBR · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Peptidoglycan-binding protein TsaP functions in surface assembly of type IV pili.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. Article
  14. 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

4 authors.

Gang LiDepartment of Microbiology and Immunology, College of Medicine, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada.
Alicia Miller
Harold Bull
S Peter Howard

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Aeromonas hydrophila secretes a number of protein toxins across the outer membrane via the type II secretion system (T2SS). Assembly of the secretion channel ExeD secretin into the outer membrane is dependent on the peptidoglycan binding domain of ExeA. In this study, the peptidoglycan binding domain PF01471 family members were divided into a prokaryotic group and a eukaryotic group. By comparison of their sequence conservation profiles and their representative crystal structures, we found the prokaryotic members to have a highly conserved pocket(s) that is not present in the eukaryotic members. Substitution mutations of nine amino acids of the pocket were constructed in ExeA. Five of the substitution derivatives showed greatly decreased lipase secretion, accompanied by defects in secretin assembly. In addition, using in vivo cross-linking and in vitro cosedimentation assays, we showed that these mutations decreased ExeA-peptidoglycan interactions. These results suggest that the highly conserved pocket in ExeA is the binding site for its peptidoglycan ligand and identify residues critical for this binding.

Indexed as

Aeromonas hydrophilaAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBinding SitesLipaseMembrane Transport ProteinsModels, MolecularMolecular Sequence DataPeptidoglycanProtein BindingProtein Structure, TertiarySecretinBacterial ProteinsExeA protein, Aeromonas hydrophilaLipaseMembrane Transport ProteinsPeptidoglycanSecretin

Identifiers

PMID20971903
PMCPMC3019969

What OpenQuestion holds

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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.