Evidence map›Paper›PMID 22155776›Full record

ArticleJournal of bacteriology2012

The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportation.

Kornelia M Mikula, Jack C Leo, Andrzej Łyskowski, Sylwia Kedracka-Krok, Artur Pirog, Adrian Goldman

Abstract read
In one paragraph

Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. A New Strain Collection for Improved Expression of Outer Membrane Proteins.Frontiers in cellular and infection microbiology · 2017
    Article
  11. Article
  12. Article
  13. Defining Potential Vaccine Targets of Haemophilus ducreyi Trimeric Autotransporter Adhesin DsrA.Monoclonal antibodies in immunodiagnosis and immunotherapy · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    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

6 authors.

Kornelia M MikulaMolecular X-Ray Crystallography Group, Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Jack C Leo
Andrzej Łyskowski
Sylwia Kedracka-Krok
Artur Pirog
Adrian Goldman

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trimeric autotransporter adhesins (TAAs) comprise one of the secretion pathways of the type V secretion system. The mechanism of their translocation across the outer membrane remains unclear, but it most probably occurs by the formation of a hairpin inside the β-barrel translocation unit, leading to transportation of the passenger domain from the C terminus to the N terminus through the lumen of the β-barrel. We further investigated the phenomenon of autotransportation and the rules that govern it. We showed by coexpressing different Escherichia coli immunoglobulin-binding (Eib) proteins that highly similar TAAs could form stochastically mixed structures (heterotrimers). We further investigated this phenomenon by coexpressing two more distantly related TAAs, EibA and YadA. These, however, did not form heterotrimers; indeed, coexpression was lethal to the cells, leading to elimination of one or another of the genes. However, substituting in either protein the barrel of the other one so that the barrels were identical led to formation of heterotrimers as for Eibs. Our work shows that trimerization of the β-barrel, but not the passenger domain, is necessary and sufficient for TAA secretion while the passenger domain is not.

Indexed as

Adhesins, BacterialBacterial AdhesionBacterial Outer Membrane ProteinsBacterial Secretion SystemsEscherichia coliEscherichia coli ProteinsMembrane ProteinsProtein BindingProtein FoldingProtein MultimerizationProtein Structure, TertiaryProtein TransportAdhesins, BacterialBacterial Outer Membrane ProteinsBacterial Secretion SystemsEibA protein, E coliEscherichia coli ProteinsMembrane Proteins

Identifiers

PMID22155776
PMCPMC3272944

What OpenQuestion holds

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Registered trials

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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.