Evidence map›Paper›PMID 23869473›Full record

ArticleMolecular microbiology2013

Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis.

Xiao-Yan Zhou, Jin-Long Gao, Neil Hunter, Jan Potempa, Ky-Anh Nguyen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. [Computer simulation of molecular docking between methylene blue and some proteins ofBeijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2022
    Article
  5. Applied and environmental microbiology · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Molecular mechanisms ofThe Japanese dental science review · 2017
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Inhibitors of bacterial protease enzymes for periodontal therapy.Clinical and experimental dental research · 2015
    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

5 authors at 3 institutions in 4 countries.

Xiao-Yan ZhouInstitute of Dental Research, Westmead Centre for Oral Health and Westmead Millennium Institute, Sydney, NSW, Australia.
Jin-Long Gao
Neil Hunter
Jan Potempa
Ky-Anh Nguyen
University of Sydney · AUMillennium Institute · BRUniversity of Louisville · US

Funding

BACTERIAL PROTEINASES IN PERIODONTAL DISEASER01DE009761 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 1991 to 2012
$3.8M
Bacterial peptidylarginine deiminase, a link between gums and joint diseaseR01DE022597 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 2013 to 2023
$3.7M
NIDCR NIH HHS DE 09761NIDCR NIH HHS R01 DE009761NIDCR NIH HHS R01 DE022597
6 · The paper itself

Abstract

The Gram-negative periodontal pathogen Porphyromonas gingivalis produces a family of outer membrane-anchored proteases, the gingipains, shown to play an essential role in virulence of the organism. The C-terminal domain (CTD) of gingipains and other secreted proteins is known to be the targeting signal for maturation and translocation of the protein through the outer membrane. The CTD is subsequently cleaved during the secretion process. Multiple alignment of various CTDs failed to define a consensus sequence at the putative CTD processing site. Using mutagenesis, we were able to show that cleavage at the site is not dependent on a specific residue and that recognition of the site is independent of local sequence. Interestingly, length of the junction between the CTD and adjacent Ig-like subdomain has a critical influence on post-translational glycan modification of the protein, whereby insertion of additional residues immediately N-terminal to the cleavage site results in failure of glycan modification and release of soluble protease into the culture medium. Various hypotheses are presented to explain these phenomena. Knowledge of the role CTDs play in maturation of gingipains has broader application for understanding maturation of CTD homologues expressed by bacteria of the Bacteriodetes phylum.

Indexed as

Protein Processing, Post-TranslationalAdhesins, BacterialAmino Acid SequenceCysteine EndopeptidasesDNA Mutational AnalysisGingipain Cysteine EndopeptidasesGlycosylationMolecular Sequence DataPorphyromonas gingivalisProtein Structure, TertiaryProtein TransportSequence AlignmentAdhesins, BacterialCysteine EndopeptidasesGingipain Cysteine Endopeptidases

Identifiers

PMID23869473
PMCPMC3773331
OpenAlexW1854259035

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.