Evidence map›Paper›PMID 31040310›Full record

ArticleScientific reports2019

Single molecule super-resolution imaging of bacterial cell pole proteins with high-throughput quantitative analysis pipeline.

Ipek Altinoglu, Christien J Merrifield, Yoshiharu Yamaichi

Abstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Superresolution imaging of antibiotic-induced structural disruption of bacteria enabled by photochromic glycomicelles.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Microfluidic Single-Cell Analytics.Advances in biochemical engineering/biotechnology · 2022
    Article
  7. Article
  8. Computerized fluorescence microscopy of microbial cells.World journal of microbiology & biotechnology · 2021
    Review
  9. Article
  10. 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

3 authors.

Ipek AltinogluDepartment of Genome Biology, Institute for Integrative Biology of the Cell (I2BC), Université Paris-Saclay, CEA, CNRS, Univ. Paris Sud, Gif sur Yvette, France.
Christien J MerrifieldDepartment of Cell Biology, Institute for Integrative Biology of the Cell (I2BC), Université Paris-Saclay, CEA, CNRS, Univ. Paris Sud, Gif sur Yvette, France.
Yoshiharu YamaichiDepartment of Genome Biology, Institute for Integrative Biology of the Cell (I2BC), Université Paris-Saclay, CEA, CNRS, Univ. Paris Sud, Gif sur Yvette, France. yoshiharu.yamaichi@i2bc.paris-saclay.fr.ORCID http://orcid.org/0000-0003-0835-5407

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria show sophisticated control of their cellular organization, and many bacteria deploy different polar landmark proteins to organize the cell pole. Super-resolution microscopy, such as Photo-Activated Localization Microscopy (PALM), provides the nanoscale localization of molecules and is crucial for better understanding of organization and dynamics in single-molecule. However, analytical tools are not fully available yet, in particular for bacterial cell biology. For example, quantitative and statistical analyses of subcellular localization with multiple cells from multiple fields of view are lacking. Furthermore, brightfield images are not sufficient to get accurate contours of small and low contrast bacterial cells, compared to subpixel presentation of target molecules. Here we describe a novel analytic tool for PALM which integrates precisely drawn cell outlines, of either inner membrane or periplasm, labelled by PALM-compatible fluorescent protein fusions, with molecule data for >10,000 molecules from >100 cells by fitting each cell into an oval arc. In the vibrioid bacterium Vibrio cholerae, the polar anchor HubP constitutes a big polar complex which includes multiple proteins involved in chemotaxis and the flagellum. With this pipeline, HubP is shown to be slightly skewed towards the inner curvature side of the cell, while its interaction partners showed rather loose polar localization.

Indexed as

Molecular ImagingSingle Molecule ImagingBacteriaBacterial ProteinsFluorescent Antibody TechniqueGene Expression Regulation, BacterialBacterial Proteins

Identifiers

PMID31040310
PMCPMC6491441

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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.