Evidence map›Paper›PMID 25858109›Full record

ArticleBiochimica et biophysica acta2015

Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members.

Iván Bárcena-Uribarri, Roland Benz, Mathias Winterhalter, Eleonora Zakharian, Nataliya Balashova

Abstract readComparative Study
In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Microorganisms · 2022
    Review
  5. Microorganisms · 2022
    Review
  6. Pathogenic determinants ofFrontiers in pediatrics · 2022
    Review
  7. Review
  8. Binding ofInternational journal of molecular sciences · 2020
    Article
  9. Pathogens (Basel, Switzerland) · 2020
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. 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 at 3 institutions in 2 countries.

Iván Bárcena-UribarriDepartment of Life Science and Chemistry, Jacobs University Bremen, Bremen, Germany.
Roland BenzDepartment of Life Science and Chemistry, Jacobs University Bremen, Bremen, Germany.
Mathias WinterhalterDepartment of Life Science and Chemistry, Jacobs University Bremen, Bremen, Germany.
Eleonora ZakharianDepartment of Cancer Biology & Pharmacology, University of Illinois College of Medicine at Peoria, Peoria, IL, USA.
Nataliya BalashovaDepartment of Pathology, School of Dental Medicine, University of Pennsylvania, Philadelphia, PA, USA. Electronic address: natbal@dental.upenn.edu.
Constructor University · DEUniversity of Illinois Urbana-Champaign · USUniversity of Pennsylvania · US

Funding

VIRULENCE FACTORS IN PERIODONTAL DISEASER01DE009517 · NIDCR · UNIVERSITY OF PENNSYLVANIA · PI BALASHOVA, NATALIYA V · 1990 to 2018
$5.2M
TRP channels in supramolecular complexes with Inorganic Polyphosphate and PolyhydR01GM098052 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI ZAKHARIAN, ELEONORA · 2011 to 2015
$1.5M
NIDCR NIH HHS R01 DE009517NIDCR NIH HHS R01DE009517NIGMS NIH HHS R01 GM098052NIGMS NIH HHS R01GM098052
6 · The paper itself

Abstract

Pediatric septic arthritis in patients under age of four is frequently caused by the oral Gram-negative bacterium Kingella kingae. This organism may be responsible for a severe form of infective endocarditis in otherwise healthy children and adults. A major virulence factor of K. kingae is RtxA, a toxin that belongs to the RTX (Repeats-in-ToXin) group of secreted pore forming toxins. To understand the RtxA effects on host cell membranes, the toxin activity was studied using planar lipid bilayers. K. kingae strain PYKK081 and its isogenic RtxA-deficient strain, KKNB100, were tested for their ability to form pores in artificial membranes of asolectin/n-decane. RtxA, purified from PYKK081, was able to rapidly form pores with an apparent diameter of 1.9nm as measured by the partition of nonelectrolytes in the pores. The RtxA channels are cation-selective and showed strong voltage-dependent gating. In contrast to supernatants of PYKK081, those of KKNB100 did not show any pore forming activity. We concluded that RtxA toxin is the only secreted protein from K. kingae forming large channels in host cell membranes where it induces cation flux leading to programmed cell death. Furthermore, our findings suggested that the planar lipid bilayer technique can effectively be used to test possible inhibitors of RTX toxin activity and to investigate the mechanism of the toxin binding to the membrane.

Indexed as

Arthritis, InfectiousBacterial ToxinsCell MembraneCytotoxinsElectrophoresis, Polyacrylamide GelHost-Pathogen InteractionsHumansInfantIon Channel GatingKingella kingaeLipid BilayersMaleMutationProtein BindingBacterial ToxinsCytotoxinsLipid BilayersBacterial pathogenesisPlanar lipid bilayerRTX-toxin

Identifiers

PMID25858109
PMCPMC4430422
OpenAlexW2083997035

What OpenQuestion holds

Textmetadata
LicenceTDM
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.