Evidence map›Paper›PMID 23955007›Full record

ArticleJournal of bacteriology2013

The D3 bacteriophage α-polymerase inhibitor (Iap) peptide disrupts O-antigen biosynthesis through mimicry of the chain length regulator Wzz in Pseudomonas aeruginosa.

Véronique L Taylor, Molly L Udaskin, Salim T Islam, Joseph S Lam

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Lipopolysaccharide-targeting treatments for multidrug-resistantExpert opinion on therapeutic targets · 2026
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  4. Directed evolution of bacteriophages: thwarted by prolific prophage.Applied and environmental microbiology · 2024
    Article
  5. [Research advances on the interaction betweenZhonghua shao shang yu chuang mian xiu fu za zhi · 2022
    Review
  6. Lipopolysaccharide O-antigens-bacterial glycans made to measure.The Journal of biological chemistry · 2020
    Review
  7. The Role ofPathogens (Basel, Switzerland) · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Adaptation ofFrontiers in microbiology · 2018
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

4 authors at 1 institution in 1 country.

Véronique L TaylorDepartment of Molecular and Cellular Biology, University of Guelph, Guelph, ON, Canada.
Molly L Udaskin
Salim T Islam
Joseph S Lam
University of Guelph · CA

Funding

Canadian Institutes of Health Research MOP-14687
6 · The paper itself

Abstract

Lysogenic bacteriophage D3 causes seroconversion of Pseudomonas aeruginosa PAO1 from serotype O5 to O16 by inverting the linkage between O-specific antigen (OSA) repeat units from α to β. The OSA units are polymerized by Wzy to modal lengths regulated by Wzz1 and Wzz2. A key component of the D3 seroconversion machinery is the inhibitor of α-polymerase (Iap) peptide, which is able to solely suppress α-linked long-chain OSA production in P. aeruginosa PAO1. To establish the target specificity of Iap for Wzyα, changes in OSA phenotypes were examined via Western immunoblotting for wzz1 and wzz2 single-knockout strains, as well as a wzz1 wzz2 double knockout, following the expression of iap from a tuneable vector. Increased induction of Iap expression completely abrogated OSA production in the wzz1 wzz2 double mutant, while background levels of OSA production were still observed in either of the single mutants. Therefore, Iap inhibition of OSA biosynthesis was most effective in the absence of both Wzz proteins. Sequence alignment analyses revealed a high degree of similarity between Iap and the first transmembrane segment (TMS) of either Wzz1 or Wzz2. Various topology prediction analyses of the Iap sequence consistently predicted the presence of a single TMS, suggesting a propensity for Iap to insert itself into the inner membrane (IM). The compromised ability of Iap to abrogate Wzyα function in the presence of Wzz1 or Wzz2 provides compelling evidence that inhibition occurs after Wzyα inserts itself into the IM and is achieved through mimicry of the first TMS from the Wzz proteins of P. aeruginosa PAO1.

Indexed as

Amino Acid SequenceAntigens, NeoplasmBacterial ProteinsBacteriophagesGene DeletionGene Expression Regulation, BacterialModels, MolecularProtein ConformationProtein Structure, TertiaryPseudomonas aeruginosaSerotypingAntigens, NeoplasmBacterial Proteinsosteosarcoma-associated antigen

Identifiers

PMID23955007
PMCPMC3807437
OpenAlexW2113338454

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.