Evidence map›Paper›PMID 25488660›Full record

ArticleThe Journal of biological chemistry2015

The inverse autotransporter intimin exports its passenger domain via a hairpin intermediate.

Philipp Oberhettinger, Jack C Leo, Dirk Linke, Ingo B Autenrieth, Monika S Schütz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

  1. Pooled it
  2. Enteric-colonizedGut microbes · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Adhesins ofPathogens (Basel, Switzerland) · 2020
    Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
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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

5 authors at 1 institution in 1 country.

Philipp OberhettingerFrom the Institut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Tübingen, Elfriede-Aulhorn-Strasse 6, 72076 Tübingen, Germany and.
Jack C Leothe Department of Biosciences, University of Oslo, P.O. Box 1066 Blindern, 0316 Oslo, Norway.
Dirk Linkethe Department of Biosciences, University of Oslo, P.O. Box 1066 Blindern, 0316 Oslo, Norway.
Ingo B AutenriethFrom the Institut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Tübingen, Elfriede-Aulhorn-Strasse 6, 72076 Tübingen, Germany and.
Monika S SchützFrom the Institut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Tübingen, Elfriede-Aulhorn-Strasse 6, 72076 Tübingen, Germany and monika.schuetz@med.uni-tuebingen.de.
University of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autotransporter proteins comprise a large family of virulence factors that consist of a β-barrel translocation unit and an extracellular effector or passenger domain. The β-barrel anchors the protein to the outer membrane of Gram-negative bacteria and facilitates the transport of the passenger domain onto the cell surface. By inserting an epitope tag into the N terminus of the passenger domain of the inverse autotransporter intimin, we generated a mutant defective in autotransport. Using this stalled mutant, we could show that (i) at the time point of stalling, the β-barrel appears folded; (ii) the stalled autotransporter is associated with BamA and SurA; (iii) the stalled intimin is decorated with large amounts of SurA; (iv) the stalled autotransporter is not degraded by periplasmic proteases; and (v) inverse autotransporter passenger domains are translocated by a hairpin mechanism. Our results suggest a function for the BAM complex not only in insertion and folding of the β-barrel but also for passenger translocation.

Indexed as

Adhesins, BacterialBiological TransportCell MembraneCloning, MolecularCross-Linking ReagentsEpitopesEscherichia coliEscherichia coli ProteinsHeLa CellsHumansMicroscopy, FluorescenceMolecular ChaperonesMutagenesis, Site-DirectedMutationPeptide HydrolasesProtein BindingAdhesins, BacterialCross-Linking ReagentseaeA protein, E coliEpitopesEscherichia coli ProteinsMolecular ChaperonesPeptide HydrolasesAdhesinBacterial PathogenesisIntimin, Type Ve Secretion, Autotransporter, beta Barrel Protein, HairpinMembrane ProteinMicrobial PathogenesisMicrobiologyOuter Membrane

Identifiers

PMID25488660
PMCPMC4340425
OpenAlexW2127159994

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.