Evidence map›Paper›PMID 21911490›Full record

ArticleThe Journal of biological chemistry2011

Characterization and scope of S-layer protein O-glycosylation in Tannerella forsythia.

Gerald Posch, Martin Pabst, Lothar Brecker, Friedrich Altmann, Paul Messner, Christina Schäffer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

60 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
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  8. The intriguing strategies ofFrontiers in oral health · 2024
    Article
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  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. A Micrarchaeon Isolate Is Covered by a Proteinaceous S-Layer.Applied and environmental microbiology · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Article
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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 2 institutions in 1 country.

Gerald PoschDepartment of NanoBiotechnology, NanoGlycobiology, Vienna Institute of BioTechnology, Universität für Bodenkultur Wien, Muthgasse 11, A-1190 Vienna, Austria.
Martin PabstDepartment of Chemistry, Vienna Institute of BioTechnology, Universität für Bodenkultur Wien, Muthgasse 18, A-1190 Vienna, Austria.
Lothar BreckerInstitute for Organic Chemistry, Universität Wien, Währingerstrasse 38, A-1090 Vienna, Austria.
Friedrich AltmannDepartment of Chemistry, Vienna Institute of BioTechnology, Universität für Bodenkultur Wien, Muthgasse 18, A-1190 Vienna, Austria.
Paul MessnerDepartment of NanoBiotechnology, NanoGlycobiology, Vienna Institute of BioTechnology, Universität für Bodenkultur Wien, Muthgasse 11, A-1190 Vienna, Austria.
Christina SchäfferDepartment of NanoBiotechnology, NanoGlycobiology, Vienna Institute of BioTechnology, Universität für Bodenkultur Wien, Muthgasse 11, A-1190 Vienna, Austria. Electronic address: christina.schaeffer@boku.ac.at.
BOKU University · ATUniversity of Vienna · AT

Funding

Austrian Science Fund FWF P 20745
6 · The paper itself

Abstract

Cell surface glycosylation is an important element in defining the life of pathogenic bacteria. Tannerella forsythia is a Gram-negative, anaerobic periodontal pathogen inhabiting the subgingival plaque biofilms. It is completely covered by a two-dimensional crystalline surface layer (S-layer) composed of two glycoproteins. Although the S-layer has previously been shown to delay the bacterium's recognition by the innate immune system, we characterize here the S-layer protein O-glycosylation as a potential virulence factor. The T. forsythia S-layer glycan was elucidated by a combination of electrospray ionization-tandem mass spectrometry and nuclear magnetic resonance spectroscopy as an oligosaccharide with the structure 4-Me-β-ManpNAcCONH(2)-(1→3)-[Pse5Am7Gc-(2→4)-]-β-ManpNAcA-(1→4)-[4-Me-α-Galp-(1→2)-]-α-Fucp-(1→4)-[-α-Xylp-(1→3)-]-β-GlcpA-(1→3)-[-β-Digp-(1→2)-]-α-Galp, which is O-glycosidically linked to distinct serine and threonine residues within the three-amino acid motif (D)(S/T)(A/I/L/M/T/V) on either S-layer protein. This S-layer glycan obviously impacts the life style of T. forsythia because increased biofilm formation of an UDP-N-acetylmannosaminuronic acid dehydrogenase mutant can be correlated with the presence of truncated S-layer glycans. We found that several other proteins of T. forsythia are modified with that specific oligosaccharide. Proteomics identified two of them as being among previously classified antigenic outer membrane proteins that are up-regulated under biofilm conditions, in addition to two predicted antigenic lipoproteins. Theoretical analysis of the S-layer O-glycosylation of T. forsythia indicates the involvement of a 6.8-kb gene locus that is conserved among different bacteria from the Bacteroidetes phylum. Together, these findings reveal the presence of a protein O-glycosylation system in T. forsythia that is essential for creating a rich glycoproteome pinpointing a possible relevance for the virulence of this bacterium.

Indexed as

BacteroidesCell MembraneChromatography, LiquidGenome, BacterialGlycopeptidesGlycosylationMagnetic Resonance SpectroscopyMembrane GlycoproteinsMonosaccharidesProteomicsSpectrometry, Mass, Electrospray IonizationSurface PropertiesTandem Mass SpectrometryVirulenceGlycopeptidesMembrane GlycoproteinsMonosaccharidesS-layer proteins

Identifiers

PMID21911490
PMCPMC3207478
OpenAlexW2028994258

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.