Evidence map›Paper›PMID 24943676›Full record

ArticleMolecular oral microbiology2014

The S-layer proteins of Tannerella forsythia are secreted via a type IX secretion system that is decoupled from protein O-glycosylation.

M B Tomek, L Neumann, I Nimeth, A Koerdt, P Andesner, P Messner, L Mach, J S Potempa, C Schäffer

Open access · greenAbstract read
In one paragraph

Article in Molecular oral microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

45 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025
    Review
  5. TheJournal of oral microbiology · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. The intriguing strategies ofFrontiers in oral health · 2024
    Article
  10. Structural Modeling of T9SS Outer Membrane Proteins and Their Complexes.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Shut-Down of Type IX Protein Secretion Alters the Host Immune Response toFrontiers in cellular and infection microbiology · 2022
    Article
  15. Article
  16. Article
  17. Article
  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

9 authors at 2 institutions in 3 countries.

M B TomekDepartment of NanoBiotechnology, NanoGlycobiology Unit, Universität für Bodenkultur Wien, Vienna, Austria.
L Neumann
I Nimeth
A Koerdt
P Andesner
P Messner
L Mach
J S Potempa
C Schäffer
BOKU University · ATUniversity of Louisville · US

Funding

BACTERIAL PROTEINASES IN PERIODONTAL DISEASER01DE009761 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 1991 to 2012
$3.8M
Austrian Science Fund FWF M 1492Austrian Science Fund FWF P 24305Austrian Science Fund FWF W 1224NIDCR NIH HHS DE 09761NIDCR NIH HHS R01 DE009761
6 · The paper itself

Abstract

Conserved C-terminal domains (CTD) have been shown to act as a signal for the translocation of certain proteins across the outer membrane of Bacteroidetes via a type IX secretion system (T9SS). The genome sequence of the periodontal pathogen Tannerella forsythia predicts the presence of the components for a T9SS in conjunction with a suite of CTD proteins. T. forsythia is covered with a two-dimensional crystalline surface (S-) layer composed of the glycosylated CTD proteins TfsA and TfsB. To investigate, if T9SS is functional in T. forsythia, T9SS-deficient mutants were generated by targeting either TF0955 (putative C-terminal signal peptidase) or TF2327 (PorK ortholog), and the mutants were analyzed with respect to secretion, assembly and glycosylation of the S-layer proteins as well as proteolytic processing of the CTD and biofilm formation. In either mutant, TfsA and TfsB were incapable of translocation, as evidenced by the absence of the S-layer in transmission electron microscopy of ultrathin-sectioned bacterial cells. Despite being entrapped within the periplasm, mass spectrometry analysis revealed that the S-layer proteins were modified with the complete, mature glycan found on the secreted proteins, indicating that protein translocation and glycosylation are two independent processes. Further, the T9SS mutants showed a denser biofilm with fewer voids compared with the wild-type. This study demonstrates the functionality of T9SS and the requirement of CTD for the outer membrane passage of extracellular proteins in T. forsythia, exemplified by the two S-layer proteins. In addition, T9SS protein translocation is decoupled from O-glycan attachment in T. forsythia.

Indexed as

Amino Acid SequenceBacterial ProteinsBacterial Secretion SystemsBacteroidetesBiofilmsGene Knockout TechniquesGlycosylationMembrane GlycoproteinsMicroscopy, Electron, ScanningMicroscopy, Electron, TransmissionMolecular Sequence DataMutationPhenotypeProtein Structure, TertiaryProtein TransportSpectrometry, Mass, Electrospray IonizationBacterial ProteinsBacterial Secretion SystemsMembrane GlycoproteinsS-layer proteinsC-terminal domainC-terminal signal peptidaseprotein secretionS-layer glycosylationT9SS

Identifiers

PMID24943676
PMCPMC4232474
OpenAlexW2029215453

What OpenQuestion holds

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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.