Evidence map›Paper›PMID 15743937›Full record

ArticleJournal of bacteriology2005

Helical disposition of proteins and lipopolysaccharide in the outer membrane of Escherichia coli.

Anindya S Ghosh, Kevin D Young

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

56 citing papers in PubMed, 82 citations in OpenAlex.

  1. The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
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  5. Article
  6. Article
  7. Review
  8. Article
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  10. Physical properties of the bacterial outer membrane.Nature reviews. Microbiology · 2022
    Review
  11. TheInternational journal of molecular sciences · 2021
    Article
  12. Phase separation in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Visualization of mycobacterial membrane dynamics in live cells.Journal of the American Chemical Society · 2017
    Article
  19. Review
  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

2 authors at 1 institution in 1 country.

Anindya S GhoshDepartment of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202-9037, USA.
Kevin D Young
University of North Dakota · US

Funding

Glycan Expression Analysis using an Odyssey CLx Infrared Imaging SystemR01GM061019 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI VOTH, DANIEL E · 2000 to 2021
$8.0M
NIGMS NIH HHS GM061019NIGMS NIH HHS R01 GM061019
6 · The paper itself

Abstract

In bacteria, several physiological processes once thought to be the products of uniformly dispersed reactions are now known to be highly asymmetric, with some exhibiting interesting geometric localizations. In particular, the cell envelope of Escherichia coli displays a form of subcellular differentiation in which peptidoglycan and outer membrane proteins at the cell poles remain stable for generations while material in the lateral walls is diluted by growth and turnover. To determine if material in the side walls was organized in any way, we labeled outer membrane proteins with succinimidyl ester-linked fluorescent dyes and then grew the stained cells in the absence of dye. Labeled proteins were not evenly dispersed in the envelope but instead appeared as helical ribbons that wrapped around the outside of the cell. By staining the O8 surface antigen of E. coli 2443 with a fluorescent derivative of concanavalin A, we observed a similar helical organization for the lipopolysaccharide (LPS) component of the outer membrane. Fluorescence recovery after photobleaching indicated that some of the outer membrane proteins remained freely diffusible in the side walls and could also diffuse into polar domains. On the other hand, the LPS O antigen was virtually immobile. Thus, the outer membrane of E. coli has a defined in vivo organization in which a subfraction of proteins and LPS are embedded in stable domains at the poles and along one or more helical ribbons that span the length of this gram-negative rod.

Indexed as

Bacterial Outer Membrane ProteinsCell MembraneConcanavalin ADiffusionEscherichia coliEscherichia coli ProteinsFluorescence Recovery After PhotobleachingLipopolysaccharidesMicroscopy, FluorescenceO AntigensPeptidoglycanProtein BindingBacterial Outer Membrane ProteinsConcanavalin AEscherichia coli ProteinsLipopolysaccharidesO AntigensPeptidoglycan

Identifiers

PMID15743937
PMCPMC1064060
OpenAlexW2132929413

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.