Evidence map›Paper›PMID 17307854›Full record

ArticleJournal of bacteriology2007

Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidis.

Andreas Knaust, Martin V R Weber, Sven Hammerschmidt, Simone Bergmann, Matthias Frosch, Oliver Kurzai

Erratum issuedAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

50 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Enolase ofFrontiers in microbiology · 2022
    Article
  8. Fibrinolysis: A Primordial System Linked to the Immune Response.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Review
  11. Review
  12. When Place Matters: Shuttling of Enolase-1 Across Cellular Compartments.Frontiers in cell and developmental biology · 2019
    Review
  13. Article
  14. Review
  15. Protein moonlighting: what is it, and why is it important?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  16. Article
  17. Review
  18. The Complement Binding and Inhibitory Protein CbiA ofFrontiers in cellular and infection microbiology · 2018
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Andreas KnaustInstitute of Hygiene and Environmental Medicine, University of Giessen, Friedrichsstrasse 16, 35392 Giessen, Germany. Andreas.Knaust@hygiene.med.uni-giessen.de
Martin V R Weber
Sven Hammerschmidt
Simone Bergmann
Matthias Frosch
Oliver Kurzai
University of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasminogen recruitment is a common strategy of pathogenic bacteria and results in a broad-spectrum surface-associated protease activity. Neisseria meningitidis has previously been shown to bind plasminogen. In this study, we show by several complementary approaches that endolase, DnaK, and peroxiredoxin, which are usually intracellular proteins, can also be located in the outer membrane and act as plasminogen receptors. Internal binding motifs, rather than C-terminal lysine residues, are responsible for plasminogen binding of the N. meningitidis receptors. Recombinant receptor proteins inhibit plasminogen association with N. meningitidis in a concentration-dependent manner. Besides binding purified plasminogen, N. meningitidis can also acquire plasminogen from human serum. Activation of N. meningitidis-associated plasminogen by urokinase results in functional activity and allows the bacteria to degrade fibrinogen. Furthermore, plasmin bound to N. meningitidis is protected against inactivation by alpha(2)-antiplasmin.

Indexed as

Amino Acid MotifsBacterial ProteinsBinding SitesCell MembraneHumansNeisseria meningitidisPeroxidasesPeroxiredoxinsPhosphopyruvate HydratasePlasminogenProtein BindingReceptors, Cell SurfaceReceptors, Urokinase Plasminogen ActivatorVirulenceBacterial ProteinsPeroxidasesPeroxiredoxinsPhosphopyruvate HydratasePlasminogenPLAUR protein, humanReceptors, Cell SurfaceReceptors, Urokinase Plasminogen Activator

Identifiers

PMID17307854
PMCPMC1855851
OpenAlexW2152673208

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.