Evidence map›Paper›PMID 22921935›Full record

ArticleMolecular cell2012

Reciprocal control between a bacterium's regulatory system and the modification status of its lipopolysaccharide.

Akinori Kato, H Deborah Chen, Tammy Latifi, Eduardo A Groisman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.3field-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

53 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Analysis of stress-induced small proteins inbioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Review
  8. Large Roles of Small Proteins.Annual review of microbiology · 2024
    Review
  9. Article
  10. PmrAB, the two-component system ofJournal of bacteriology · 2024
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Small Proteins; Big Questions.Journal of bacteriology · 2022
    Article
  16. How the PhoP/PhoQ System Controls Virulence and MgMicrobiology and molecular biology reviews : MMBR · 2021
    Review
  17. Review
  18. Article
  19. LpxT-Dependent Phosphorylation of Lipid A inFrontiers in microbiology · 2021
    Article
  20. 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

4 authors at 3 institutions in 2 countries.

Akinori KatoHoward Hughes Medical Institute, Washington University School of Medicine, St. Louis, MO 63110, USA.
H Deborah Chen
Tammy Latifi
Eduardo A Groisman
Washington University in St. Louis · USHoward Hughes Medical Institute · USYale University · US

Funding

MOLECULAR AND STRUCTURAL BASES OF POLYMYXIN RESISTANCER01AI042236 · NIAID · YALE UNIVERSITY · PI GROISMAN, EDUARDO · 1998 to 2013
$3.0M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI042236PHS HHS 42336
6 · The paper itself

Abstract

Gram-negative bacteria often modify their lipopolysaccharide (LPS), thereby increasing resistance to antimicrobial agents and avoidance of the host immune system. However, it is unclear how bacteria adjust the levels and activities of LPS-modifying enzymes in response to the modification status of their LPS. We now address this question by investigating the major regulator of LPS modifications in Salmonella enterica. We report that the PmrA/PmrB system controls expression of a membrane peptide that inhibits the activity of LpxT, an enzyme responsible for increasing the LPS negative charge. LpxT's inhibition and the PmrA-dependent incorporation of positively charged L-4-aminoarabinose into the LPS decrease Fe(3+) binding to the bacterial cell. Because Fe(3+) is an activating ligand for the sensor PmrB, transcription of PmrA-dependent LPS-modifying genes is reduced. This mechanism enables bacteria to sense their cell surface by its effect on the availability of an inducing signal for the system regulating cell-surface modifications.

Indexed as

Salmonella typhimuriumAnti-Bacterial AgentsArabinoseBacterial ProteinsCell MembraneFerric CompoundsGene Expression Regulation, BacterialLipopolysaccharidesPhosphotransferases (Phosphate Group Acceptor)Signal TransductionTranscription FactorsaminoarabinoseAnti-Bacterial AgentsArabinoseBacterial ProteinsFerric CompoundsLipopolysaccharidesPhosphotransferases (Phosphate Group Acceptor)pmrA protein, BacteriaPmrB protein, bacteriaTranscription Factors

Identifiers

PMID22921935
PMCPMC3465083
OpenAlexW1982760680

What OpenQuestion holds

Textmetadata
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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.