Evidence map›Paper›PMID 23243304›Full record

ArticleJournal of bacteriology2013

Calcium binding properties of the Kingella kingae PilC1 and PilC2 proteins have differential effects on type IV pilus-mediated adherence and twitching motility.

Eric A Porsch, Michael D L Johnson, Angela D Broadnax, Christopher K Garrett, Matthew R Redinbo, Joseph W St Geme

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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Deciphering the enigmatic PilY1 ofBiochemistry and biophysics reports · 2024
    Article
  5. TheInfection and immunity · 2023
    Article
  6. Microorganisms · 2022
    Review
  7. Pharyngeal Colonization byMicroorganisms · 2022
    Review
  8. Article
  9. A noncanonical cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Pathogenic determinants ofFrontiers in pediatrics · 2022
    Review
  11. PilB fromProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. PilY1 PromotesFrontiers in cellular and infection microbiology · 2017
    Article
  16. Editorial.FEMS microbiology reviews · 2015
    Article
  17. Review
  18. Kingella kingae: carriage, transmission, and disease.Clinical microbiology reviews · 2015
    Review
  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

6 authors at 3 institutions in 1 country.

Eric A PorschDepartment of Pediatrics, Duke University Medical Center, Durham, NC, USA.
Michael D L Johnson
Angela D Broadnax
Christopher K Garrett
Matthew R Redinbo
Joseph W St Geme
University of North Carolina at Chapel Hill · USDuke Medical Center · USDuke University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kingella kingae is an emerging bacterial pathogen that is being recognized increasingly as an important etiology of septic arthritis, osteomyelitis, and bacteremia, especially in young children. The pathogenesis of K. kingae disease begins with bacterial adherence to respiratory epithelium, which is dependent on type IV pili and is influenced by two PilC-like proteins called PilC1 and PilC2. Production of either PilC1 or PilC2 is necessary for K. kingae piliation and bacterial adherence. In this study, we set out to further investigate the role of PilC1 and PilC2 in type IV pilus-associated phenotypes. We found that PilC1 contains a functional 9-amino-acid calcium-binding (Ca-binding) site with homology to the Pseudomonas aeruginosa PilY1 Ca-binding site and that PilC2 contains a functional 12-amino-acid Ca-binding site with homology to the human calmodulin Ca-binding site. Using targeted mutagenesis to disrupt the Ca-binding sites, we demonstrated that the PilC1 and PilC2 Ca-binding sites are dispensable for piliation. Interestingly, we showed that the PilC1 site is necessary for twitching motility and adherence to Chang epithelial cells, while the PilC2 site has only a minor influence on twitching motility and no influence on adherence. These findings establish key differences in PilC1 and PilC2 function in K. kingae and provide insights into the biology of the PilC-like family of proteins.

Indexed as

Bacterial AdhesionBinding SitesCalciumFimbriae, BacterialFimbriae ProteinsGene Expression Regulation, BacterialKingella kingaeMovementPhenotypePlasmidsProtein BindingCalciumFimbriae Proteins

Identifiers

PMID23243304
PMCPMC3562114
OpenAlexW2141394177

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.