Evidence map›Paper›PMID 24002068›Full record

ArticleInfection and immunity2013

Mutation of the conserved calcium-binding motif in Neisseria gonorrhoeae PilC1 impacts adhesion but not piliation.

Yuan Cheng, Michael D L Johnson, Christine Burillo-Kirch, Jeffrey C Mocny, James E Anderson, Christopher K Garrett, Matthew R Redinbo, Christopher E Thomas

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 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
2.4field-weighted citation impact, top 12% 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, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. A noncanonical cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Calcium Regulation of Bacterial Virulence.Advances in experimental medicine and biology · 2020
    Review
  9. Review
  10. Article
  11. PilY1 PromotesFrontiers in cellular and infection microbiology · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Editorial.FEMS microbiology reviews · 2015
    Article
  17. 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 1 institution in 1 country.

Yuan ChengDepartment of Medicine, Division of Infectious Diseases.
Michael D L Johnson
Christine Burillo-Kirch
Jeffrey C Mocny
James E Anderson
Christopher K Garrett
Matthew R Redinbo
Christopher E Thomas
University of North Carolina at Chapel Hill · US

Funding

Trichomonas Typing SystemU19AI031496 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI HOBBS, MARCIA METZGAR · 1995 to 2014
$24.9M
Structure and Inhibition of the Conjugative DNA Relaxase-HelicaseR01AI078924 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI REDINBO, MATTHEW R · 2008 to 2012
$1.9M
NIAID NIH HHS R01 AI078924NIAID NIH HHS R01 AI78924NIAID NIH HHS U19 AI031496
6 · The paper itself

Abstract

Neisseria gonorrhoeae PilC1 is a member of the PilC family of type IV pilus-associated adhesins found in Neisseria species and other type IV pilus-producing genera. Previously, a calcium-binding domain was described in the C-terminal domains of PilY1 of Pseudomonas aeruginosa and in PilC1 and PilC2 of Kingella kingae. Genetic analysis of N. gonorrhoeae revealed a similar calcium-binding motif in PilC1. To evaluate the potential significance of this calcium-binding region in N. gonorrhoeae, we produced recombinant full-length PilC1 and a PilC1 C-terminal domain fragment. We show that, while alterations of the calcium-binding motif disrupted the ability of PilC1 to bind calcium, they did not grossly affect the secondary structure of the protein. Furthermore, we demonstrate that both full-length wild-type PilC1 and full-length calcium-binding-deficient PilC1 inhibited gonococcal adherence to cultured human cervical epithelial cells, unlike the truncated PilC1 C-terminal domain. Similar to PilC1 in K. kingae, but in contrast to the calcium-binding mutant of P. aeruginosa PilY1, an equivalent mutation in N. gonorrhoeae PilC1 produced normal amounts of pili. However, the N. gonorrhoeae PilC1 calcium-binding mutant still had partial defects in gonococcal adhesion to ME180 cells and genetic transformation, which are both essential virulence factors in this human pathogen. Thus, we conclude that calcium binding to PilC1 plays a critical role in pilus function in N. gonorrhoeae.

Indexed as

Bacterial AdhesionAdhesins, BacterialBinding SitesCalciumCell LineDNA Mutational AnalysisEpithelial CellsFimbriae, BacterialFimbriae ProteinsHumansMutant ProteinsNeisseria gonorrhoeaeProtein ConformationProtein Structure, TertiaryAdhesins, BacterialCalciumFimbriae ProteinsMutant ProteinspilC protein, Neisseria gonorrhoeae

Identifiers

PMID24002068
PMCPMC3811810
OpenAlexW2162268598

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.