Evidence map›Paper›PMID 21255118›Full record

ArticleMolecular microbiology2011

In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae.

Miranda D Gray, Michael Bagdasarian, Wim G J Hol, Maria Sandkvist

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Landmark Discoveries and Recent Advances in Type IV Pilus Research.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Lipid-Modified Azurin ofFrontiers in microbiology · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Editorial.FEMS microbiology reviews · 2015
    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

4 authors at 2 institutions in 1 country.

Miranda D GrayUniversity of Michigan Medical School, Department of Microbiology and Immunology, Ann Arbor, MI 48109, USA.
Michael Bagdasarian
Wim G J Hol
Maria Sandkvist
Michigan State University · USUniversity of Washington · US

Funding

Molecular Mechanisms of Microbial Pathogenesis Training ProgramT32AI007528 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CARRUTHERS, VERNON BRUCE · 1998 to 2024
$6.8M
STRUCTURAL STUDY OF HEAT-LABILE ENTEROTOXINR01AI034501 · NIAID · UNIVERSITY OF WASHINGTON · PI HOL, WILHELMUS G. J. · 1993 to 2013
$5.4M
Organization and Function of a Type II Secretion ComplexR01AI049294 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SANDKVIST, MARIA B · 2002 to 2012
$2.9M
Targeting type II secretion, a common virulence pathwayR01AI081705 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SANDKVIST, MARIA B · 2009 to 2010
$760k
NIAID NIH HHS AI007528NIAID NIH HHS R01 AI034501NIAID NIH HHS R01 AI049294NIAID NIH HHS R01AI049294NIAID NIH HHS R01 AI081705NIAID NIH HHS R01AI081705NIAID NIH HHS R01AI34501NIAID NIH HHS T32 AI007528
6 · The paper itself

Abstract

The type II secretion system is a multi-protein complex that spans the cell envelope of Gram-negative bacteria and promotes the secretion of proteins, including several virulence factors. This system is homologous to the type IV pilus biogenesis machinery and contains five proteins, EpsG-K, termed the pseudopilins that are structurally homologous to the type IV pilins. The major pseudopilin EpsG has been proposed to form a pilus-like structure in an energy-dependent process that requires the ATPase, EpsE. A key remaining question is how the membrane-bound EpsG interacts with the cytoplasmic ATPase, and if this is a direct or indirect interaction. Previous studies have established an interaction between the bitopic inner membrane protein EpsL and EpsE; therefore, in this study we used in vivo cross-linking to test the hypothesis that EpsG interacts with EpsL. Our findings suggest that EpsL may function as a scaffold to link EpsG and EpsE and thereby transduce the energy generated by ATP hydrolysis to support secretion. The recent discovery of structural homology between EpsL and a protein in the type IV pilus system implies that this interaction may be conserved and represent an important functional interaction for both the type II secretion and type IV pilus systems.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsCross-Linking ReagentsFimbriae ProteinsImmunoprecipitationModels, MolecularMutationProtein BindingProtein Processing, Post-TranslationalThreonineVibrio choleraeAdenosine TriphosphatasesBacterial ProteinsCross-Linking ReagentsFimbriae ProteinsThreonine

Identifiers

PMID21255118
PMCPMC3044931
OpenAlexW2167883670

What OpenQuestion holds

Textmetadata
LicenceTDM
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.