Evidence map›Paper›PMID 17951381›Full record

ArticleJournal of bacteriology2008

Genetic and functional analyses of PptA, a phospho-form transferase targeting type IV pili in Neisseria gonorrhoeae.

Cecilia L Naessan, Wolfgang Egge-Jacobsen, Ryan W Heiniger, Matthew C Wolfgang, Finn Erik Aas, Asmund Røhr, Hanne C Winther-Larsen, Michael Koomey

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

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  11. Identification ofFrontiers in microbiology · 2017
    Article
  12. Isolation and characterization of Neisseria musculi sp. nov., from the wild house mouse.International journal of systematic and evolutionary microbiology · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Type IV pilin proteins: versatile molecular modules.Microbiology and molecular biology reviews : MMBR · 2012
    Review
  18. Article
  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

8 authors at 2 institutions in 2 countries.

Cecilia L NaessanDepartment of Molecular Biosciences, Centre for Molecular Biology and Neuroscience, University of Oslo, 0316 Oslo, Norway.
Wolfgang Egge-Jacobsen
Ryan W Heiniger
Matthew C Wolfgang
Finn Erik Aas
Asmund Røhr
Hanne C Winther-Larsen
Michael Koomey
University of Oslo · NOUniversity of North Carolina at Chapel Hill · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PilE pilin subunit protein of Neisseria gonorrhoeae undergoes unique covalent modifications with phosphoethanolamine (PE) and phosphocholine (PC). The pilin phospho-form transferase A (PptA) protein, required for these modifications, shows sequence relatedness with and architectural similarities to lipopolysaccharide PE transferases. Here, we used regulated expression and mutagenesis as means to better define the relationships between PptA structure and function, as well as to probe the mechanisms by which other factors impact the system. We show here that pptA expression is coupled at the level of transcription to its distal gene, murF, in a division/cell wall gene operon and that PptA can act in a dose-dependent fashion in PilE phospho-form modification. Molecular modeling and site-directed mutagenesis provided the first direct evidence that PptA is a member of the alkaline phosphatase superfamily of metalloenzymes with similar metal-binding sites and conserved structural folds. Through phylogenetic analyses and sequence alignments, these conclusions were extended to include the lipopolysaccharide PE transferases, including members of the disparate Lpt6 subfamily, and the MdoB family of phosphoglycerol transferases. Each of these enzymes thus likely acts as a phospholipid head group transferase whose catalytic mechanism involves a trans-esterification step generating a protein-phospho-form ester intermediate. Coexpression of PptA with PilE in Pseudomonas aeruginosa resulted in high levels of PE modification but was not sufficient for PC modification. This and other findings show that PptA-associated PC modification is governed by as-yet-undefined ancillary factors unique to N. gonorrhoeae.

Indexed as

Anti-Bacterial AgentsFimbriae, BacterialGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicImmunoblottingMicrobial Sensitivity TestsMutagenesisNeisseria gonorrhoeaePlasmidsPromoter Regions, GeneticPseudomonas aeruginosaRecombinant ProteinsTransferases (Other Substituted Phosphate Groups)Anti-Bacterial AgentsPptA protein, Neisseria meningitidisRecombinant ProteinsTransferases (Other Substituted Phosphate Groups)

Identifiers

PMID17951381
PMCPMC2223744
OpenAlexW2124559749

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.