Evidence map›Paper›PMID 22267511›Full record

ArticleJournal of bacteriology2012

Resistance phenotypes mediated by aminoacyl-phosphatidylglycerol synthases.

Wiebke Arendt, Stefanie Hebecker, Sonja Jäger, Manfred Nimtz, Jürgen Moser

Abstract read
In one paragraph

Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Small-Molecule Acetylation by GCN5-RelatedMicrobiology and molecular biology reviews : MMBR · 2020
    Review
  10. Review
  11. Article
  12. Lipids in the cell: organisation regulates function.Cellular and molecular life sciences : CMLS · 2018
    Review
  13. Review
  14. Identification ofFrontiers in microbiology · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Lantibiotic resistance.Microbiology and molecular biology reviews : MMBR · 2015
    Review
  19. 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.

Wiebke ArendtInstitute of Microbiology, Technische Universität Braunschweig, Braunschweig, Germany.
Stefanie Hebecker
Sonja Jäger
Manfred Nimtz
Jürgen Moser

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The specific aminoacylation of the phospholipid phosphatidylglycerol (PG) with alanine or with lysine catalyzed by aminoacyl-phosphatidylglycerol synthases (aaPGS) was shown to render various organisms less susceptible to antibacterial agents. This study makes use of Pseudomonas aeruginosa chimeric mutant strains producing lysyl-phosphatidylglycerol (L-PG) instead of the naturally occurring alanyl-phosphatidylglycerol (A-PG) to study the resulting impact on bacterial resistance. Consequences of such artificial phospholipid composition were studied in the presence of an overall of seven antimicrobials (β-lactams, a lipopeptide antibiotic, cationic antimicrobial peptides [CAMPs]) to quantitatively assess the effect of A-PG substitution (with L-PG, L-PG and A-PG, increased A-PG levels). For the employed Gram-negative P. aeruginosa model system, an exclusive charge repulsion mechanism does not explain the attenuated antimicrobial susceptibility due to PG modification. Additionally, the specificity of nine orthologous aaPGS enzymes was experimentally determined. The newly characterized protein sequences allowed for the establishment of a significant group of A-PG synthase sequences which were bioinformatically compared to the related group of L-PG synthesizing enzymes. The analysis revealed a diverse origin for the evolution of A-PG and L-PG synthases, as the specificity of an individual enzyme is not reflected in terms of a characteristic sequence motif. This finding is relevant for future development of potential aaPGS inhibitors.

Indexed as

Drug Resistance, BacterialAlanineAminoacyltransferasesAnti-Bacterial AgentsBacterial ProteinsLysineMicrobial Sensitivity TestsPhosphatidylglycerolsPhylogenyPseudomonas aeruginosaRecombinant ProteinsSequence Homology, Amino AcidAlaninealanyl-phosphatidylglycerol synthase, Pseudomonas aeruginosaAminoacyltransferasesAnti-Bacterial AgentsBacterial ProteinsLysinePhosphatidylglycerolsRecombinant Proteins

Identifiers

PMID22267511
PMCPMC3294870

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.