Evidence map›Paper›PMID 18316383›Full record

ArticleInfection and immunity2008

Role of RppA in the regulation of polymyxin b susceptibility, swarming, and virulence factor expression in Proteus mirabilis.

Won-Bo Wang, I-Chun Chen, Sin-Sien Jiang, Hui-Ru Chen, Chia-Yu Hsu, Po-Ren Hsueh, Wei-Bin Hsu, Shwu-Jen Liaw

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
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  4. Unveiling the hidden arsenal: new insights intoFrontiers in cellular and infection microbiology · 2024
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  8. Into the understanding the multicellular lifestyle ofFrontiers in cellular and infection microbiology · 2022
    Review
  9. De-repression of theAntimicrobial agents and chemotherapy · 2019
    Article
  10. Article
  11. Article
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  13. Article
  14. Polymyxin: Alternative Mechanisms of Action and Resistance.Cold Spring Harbor perspectives in medicine · 2016
    Review
  15. Article
  16. Review
  17. Article
  18. 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

8 authors at 2 institutions in 1 country.

Won-Bo WangGraduate Institute of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan University, Taipei, Taiwan, Republic of China.
I-Chun Chen
Sin-Sien Jiang
Hui-Ru Chen
Chia-Yu Hsu
Po-Ren Hsueh
Wei-Bin Hsu
Shwu-Jen Liaw
National Taiwan University · TWNational Taiwan University Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteus mirabilis, a human pathogen that frequently causes urinary tract infections, is intrinsically highly resistant to cationic antimicrobial peptides, such as polymyxin B (PB). To explore the mechanisms underlying P. mirabilis resistance to PB, a mutant which displayed increased (> 160-fold) sensitivity to PB was identified by transposon mutagenesis. This mutant was found to have Tn5 inserted into a novel gene, rppA. Sequence analysis indicated that rppA may encode a response regulator of the two-component system and is located upstream of the rppB gene, which may encode a membrane sensor kinase. An rppA knockout mutant of P. mirabilis had an altered lipopolysaccharide (LPS) profile. The LPS purified from the rppA knockout mutant could bind more PB than the LPS purified from the wild type. These properties of the rppA knockout mutant may contribute to its PB-sensitive phenotype. The rppA knockout mutant exhibited greater swarming motility and cytotoxic activity and expressed higher levels of flagellin and hemolysin than the wild type, suggesting that RppA negatively regulates swarming, hemolysin expression, and cytotoxic activity in P. mirabilis. PB could modulate LPS synthesis and modification, swarming, hemolysin expression, and cytotoxic activity in P. mirabilis through an RppA-dependent pathway, suggesting that PB could serve as a signal to regulate RppA activity. Finally, we demonstrated that the expression of rppA was up-regulated by a low concentration of PB and down-regulated by a high concentration of Mg2+. Together, these data highlight the essential role of RppA in regulating PB susceptibility and virulence functions in P. mirabilis.

Indexed as

Drug Resistance, BacterialGene Expression Regulation, BacterialLocomotionAnti-Bacterial AgentsBacterial ProteinsCell LineDNA, BacterialDNA Transposable ElementsFlagellinGene DeletionHemolysin ProteinsHumansLipopolysaccharidesMolecular Sequence DataMutagenesis, InsertionalPolymyxin BAnti-Bacterial AgentsBacterial ProteinsDNA, BacterialDNA Transposable ElementsFlagellinHemolysin ProteinsLipopolysaccharidesPolymyxin BRppA protein, SynechocystisVirulence Factors

Identifiers

PMID18316383
PMCPMC2346679
OpenAlexW2026552684

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.