Evidence map›Paper›PMID 19251862›Full record

ArticleJournal of bacteriology2009

Docking and assembly of the type II secretion complex of Vibrio cholerae.

Suzanne R Lybarger, Tanya L Johnson, Miranda D Gray, Aleksandra E Sikora, Maria Sandkvist

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Defining Assembly Pathways by Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Tracking Proteins Secreted by Bacteria: What's in the Toolbox?Frontiers in cellular and infection microbiology · 2017
    Review
  12. Review
  13. Shedding light on biology of bacterial cells.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Editorial.FEMS microbiology reviews · 2015
    Article
  20. 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

5 authors at 1 institution in 1 country.

Suzanne R LybargerDept. of Microbiology and Immunology, University of Michigan Medical School, 1150 West Medical Center Drive, Ann Arbor, MI 48109, USA.
Tanya L Johnson
Miranda D Gray
Aleksandra E Sikora
Maria Sandkvist
University of Michigan–Ann Arbor · US

Funding

Vascular Biology Training ProgramT32HL007698 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI Rosemary A Kozar, Dudley K. Strickland · 1991 to 2026
$8.7M
Molecular Mechanisms of Microbial Pathogenesis Training ProgramT32AI007528 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CARRUTHERS, VERNON BRUCE · 1998 to 2024
$6.8M
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
Organization and function of a type II secretion complexR56AI049294 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SANDKVIST, MARIA B · 2015 to 2015
$393k
NHLBI NIH HHS HL007698NHLBI NIH HHS T32 HL007698NIAID NIH HHS AI007258NIAID NIH HHS AI49294NIAID NIH HHS R01 AI049294NIAID NIH HHS R56 AI049294NIAID NIH HHS T32 AI007528
6 · The paper itself

Abstract

Secretion of cholera toxin and other virulence factors from Vibrio cholerae is mediated by the type II secretion (T2S) apparatus, a multiprotein complex composed of both inner and outer membrane proteins. To better understand the mechanism by which the T2S complex coordinates translocation of its substrates, we are examining the protein-protein interactions of its components, encoded by the extracellular protein secretion (eps) genes. In this study, we took a cell biological approach, observing the dynamics of fluorescently tagged EpsC and EpsM proteins in vivo. We report that the level and context of fluorescent protein fusion expression can have a bold effect on subcellular location and that chromosomal, intraoperon expression conditions are optimal for determining the intracellular locations of fusion proteins. Fluorescently tagged, chromosomally expressed EpsC and EpsM form discrete foci along the lengths of the cells, different from the polar localization for green fluorescent protein (GFP)-EpsM previously described, as the fusions are balanced with all their interacting partner proteins within the T2S complex. Additionally, we observed that fluorescent foci in both chromosomal GFP-EpsC- and GFP-EpsM-expressing strains disperse upon deletion of epsD, suggesting that EpsD is critical to the localization of EpsC and EpsM and perhaps their assembly into the T2S complex.

Indexed as

Artificial Gene FusionBacterial ProteinsCell MembraneCholera ToxinGene DeletionGenes, ReporterGreen Fluorescent ProteinsMembrane ProteinsMembrane Transport ProteinsMicroscopy, FluorescenceProtein BindingProtein Interaction MappingRecombinant Fusion ProteinsVibrio choleraeBacterial ProteinsCholera ToxinEpsD protein, Vibrio choleraeEpsM protein, Vibrio choleraeGreen Fluorescent ProteinsMembrane ProteinsMembrane Transport ProteinsRecombinant Fusion Proteins

Identifiers

PMID19251862
PMCPMC2681814
OpenAlexW2117165918

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.