Evidence map›Paper›PMID 21040511›Full record

ArticleMolecular oral microbiology2010

Characterization of a novel family of fibronectin-binding proteins with M23 peptidase domains from Treponema denticola.

C V Bamford, T Francescutti, C E Cameron, H F Jenkinson, D Dymock

Open access · greenAbstract read
In one paragraph

Article in Molecular oral microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Infection and immunity · 2026
    Review
  3. Review
  4. Participants inFrontiers in immunology · 2025
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. NovelBioMed research international · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. That's my story, and I'm sticking to it--an update on B. burgdorferi adhesins.Frontiers in cellular and infection microbiology · 2014
    Review
  15. Article
  16. Article
  17. Article
  18. Treponema denticola interactions with host proteins.Journal of oral microbiology · 2012
    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.

C V BamfordOral Microbiology Unit, Department of Oral and Dental Science, University of Bristol, Bristol, UK. caroline.bamford@bristol.ac.uk
T Francescutti
C E Cameron
H F Jenkinson
D Dymock
University of Bristol · GBUniversity of Victoria · CAUniversity Of Bristol Dental Hospital · GB

Funding

Extracellular Matrix Adhesins of Treponema pallidumR01AI051334 · NIAID · UNIVERSITY OF WASHINGTON · PI CAMERON, CAROLINE E · 2002 to 2017
$3.4M
NIAID NIH HHS R01 AI051334
6 · The paper itself

Abstract

Interactions with fibronectin are important in the virulence strategies of a range of disease-related bacteria. The periodontitis-associated oral spirochaete Treponema denticola expresses at least two fibronectin-binding proteins, designated Msp (major surface protein) and OppA (oligopeptide-binding protein homologue). To identify other T. denticola outer membrane fibronectin-binding proteins, the amino acid sequence of the Treponema pallidum fibronectin-binding protein Tp0155 was used to survey the T. denticola genome. Seven T. denticola genes encoding orthologous proteins were identified. All but two were expressed in Escherichia coli and purified recombinant proteins bound fibronectin. Using antibodies to the N-terminal region of Tp0155, it was demonstrated that T. denticola TDE2318, with highest homology to Tp0155, was cell surface localized. Like Tp0155, the seven T. denticola proteins contained an M23 peptidase domain and four (TDE2318, TDE2753, TDE1738, TDE1297) contained one or two LysM domains. M23 peptidases can degrade peptidoglycan whereas LysM domains recognize carbohydrate polymers. In addition, TDE1738 may act as a bacteriocin based on homology with other bacterial lysins and the presence of an adjacent gene encoding a putative immunity factor. Collectively, these results suggest that T. denticola expresses fibronectin-binding proteins associated with the cell surface that may also have cell wall modifying or lytic functions.

Indexed as

Adhesins, BacterialAmino Acid MotifsBacterial AdhesionBacterial Outer Membrane ProteinsBacterial ProteinsBacteriocinsBlotting, WesternCarrier ProteinsConsensus SequenceElectrophoresis, Polyacrylamide GelEscherichia coliFibronectinsGenome, BacterialHumansLipoproteinsMembrane ProteinsAdhesins, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsBacteriocinsCarrier Proteinsfibronectin-binding proteins, bacterialFibronectinsLipoproteinsMembrane Proteinsoligopeptide-binding protein, bacteriaOligopeptidesPeptide HydrolasesPeptidoglycan

Identifiers

PMID21040511
PMCPMC3103763
OpenAlexW2112034189

What OpenQuestion holds

Textmetadata
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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.