Evidence map›Paper›PMID 27103580›Full record

ArticleScientific reports2016

VirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalis.

Christian Fercher, Ines Probst, Verena Kohler, Nikolaus Goessweiner-Mohr, Karsten Arends, Elisabeth Grohmann, Klaus Zangger, N Helge Meyer, Walter Keller

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. 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
3.6field-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

14 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. The type IV secretion system ofMicrobial genomics · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
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  11. VirB8 homolog TraE from plasmid pKM101 forms a hexameric ring structure and interacts with the VirB6 homolog TraD.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Review
  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

9 authors at 6 institutions in 2 countries.

Christian FercherInstitute of Molecular Biosciences, NAWI Graz, University of Graz, Austria.
Ines ProbstDivision of Infectious Diseases, University Medical Center Freiburg, Germany.
Verena KohlerInstitute of Molecular Biosciences, NAWI Graz, University of Graz, Austria.
Nikolaus Goessweiner-MohrCenter for Structural System Biology (CSSB), University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany.
Karsten ArendsRobert Koch Institute, Berlin, Germany.
Elisabeth GrohmannDivision of Infectious Diseases, University Medical Center Freiburg, Germany.
Klaus ZanggerInstitute of Chemistry, University of Graz, Graz, Austria.
N Helge MeyerDepartment of General and Visceral Surgery, University of Oldenburg, Germany.
Walter KellerInstitute of Molecular Biosciences, NAWI Graz, University of Graz, Austria.
Nawi Graz · ATUniversity Medical Center Freiburg · DEUniversity of Graz · ATCarl von Ossietzky Universität Oldenburg · DERobert Koch Institute · DEUniversity Medical Center Hamburg-Eppendorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Untreatable bacterial infections caused by a perpetual increase of antibiotic resistant strains represent a serious threat to human healthcare in the 21(st) century. Conjugative DNA transfer is the most important mechanism for antibiotic resistance and virulence gene dissemination among bacteria and is mediated by a protein complex, known as type IV secretion system (T4SS). The core of the T4SS is a multiprotein complex that spans the bacterial envelope as a channel for macromolecular secretion. We report the NMR structure and functional characterization of the transfer protein TraH encoded by the conjugative Gram-positive broad-host range plasmid pIP501. The structure exhibits a striking similarity to VirB8 proteins of Gram-negative secretion systems where they play an essential role in the scaffold of the secretion machinery. Considering TraM as the first VirB8-like protein discovered in pIP501, TraH represents the second protein affiliated with this family in the respective transfer operon. A markerless traH deletion in pIP501 resulted in a total loss of transfer in Enterococcus faecalis as compared with the pIP501 wild type (wt) plasmid, demonstrating that TraH is essential for pIP501 mediated conjugation. Moreover, oligomerization state and topology of TraH in the native membrane were determined providing insights in molecular organization of a Gram-positive T4SS.

Indexed as

Biological TransportConjugation, GeneticGene Transfer, HorizontalBacterial ProteinsDNAEnterococcus faecalisGene DeletionHumansMagnetic Resonance SpectroscopyNuclear ProteinsPlasmidsProtein ConformationBacterial ProteinsDNANuclear ProteinsTraH protein, Bacteria

Identifiers

PMID27103580
PMCPMC4840375
OpenAlexW2341470594

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LicenceCC BY
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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.