Evidence map›Paper›PMID 20736171›Full record

ArticleThe Journal of biological chemistry2010

The role of the exopolyphosphatase PPX in avoidance by Neisseria meningitidis of complement-mediated killing.

Qian Zhang, Yanwen Li, Christoph M Tang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Gallein and isoniazid act synergistically to attenuatebioRxiv : the preprint server for biology · 2024
    Article
  3. Article
  4. Bacteriophage steering ofJournal of bacteriology · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Polyphosphates and Complement Activation.Frontiers in medicine · 2019
    Review
  11. Polyphosphate in thrombosis, hemostasis, and inflammation.Research and practice in thrombosis and haemostasis · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  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

3 authors at 1 institution in 1 country.

Qian ZhangDepartment of Microbiology, Centre for Molecular Microbiology and Infection, Flowers Building, Imperial College London, London SW7 2AZ, United Kingdom.
Yanwen Li
Christoph M Tang
Imperial College London · GB

Funding

Medical Research Council G0900888
6 · The paper itself

Abstract

The complement system is critical for immunity against the important human pathogen Neisseria meningitidis. We describe the isolation of a meningococcal mutant lacking PPX, an exopolyphosphatase responsible for cleaving cellular polyphosphate, a polymer of tens to hundreds of orthophosphate residues found in virtually all living cells. Bacteria lacking PPX exhibit increased resistance to complement-mediated killing. By site directed mutagenesis, we define amino acids necessary for the biochemical activity of meningococcal PPX, including a conserved glutamate (Glu(117)) and residues in the Walker B box predicted to be involved in binding to phosphate. We show that the biochemical activity of PPX is necessary for interactions with the complement. The relative resistance of the ppx mutant does not result from changes in structures (such as capsule, lipopolysaccharide, and factor H-binding protein), which are known to be required for evasion of this key aspect of host immunity. Instead, expression of PPX modifies the interaction of N. meningitidis with the alternative pathway of complement activation.

Indexed as

Acid Anhydride HydrolasesAmino Acid SequenceComplement System ProteinsGlutamic AcidHumansLipopolysaccharidesMolecular Sequence DataMutagenesis, Site-DirectedNeisseria meningitidisOligonucleotidesPhosphoric Monoester HydrolasesPlasmidsPolymerase Chain ReactionProtein Structure, TertiarySequence Homology, Amino AcidAcid Anhydride HydrolasesComplement System ProteinsexopolyphosphataseGlutamic AcidLipopolysaccharidesOligonucleotidesPhosphoric Monoester Hydrolases

Identifiers

PMID20736171
PMCPMC2962524
OpenAlexW1989919343

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.