Evidence map›Paper›PMID 23258847›Full record

ArticleGlycobiology2013

"Cross-glycosylation" of proteins in Bacteroidales species.

Gerald Posch, Martin Pabst, Laura Neumann, Michael J Coyne, Friedrich Altmann, Paul Messner, Laurie E Comstock, Christina Schäffer

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2013. 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
1.2field-weighted citation impact, top 22% 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, 30 citations in OpenAlex.

  1. Structural basis of iron piracy by human gutProceedings of the National Academy of Sciences of the United States of America · 2026
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  2. Review
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  4. Characterization of theJournal of bacteriology · 2023
    Article
  5. Article
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  8. Loss ofmSphere · 2019
    Article
  9. A General ProteinFrontiers in microbiology · 2018
    Article
  10. Article
  11. Article
  12. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  13. Article
  14. Article
  15. The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  16. Review
  17. Article
  18. Bacterial cell-envelope glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2013
    Review
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 2 institutions in 2 countries.

Gerald PoschDepartment of NanoBiotechnology, NanoGlycobiology Unit, Universität für Bodenkultur Wien, Muthgasse 11, 1190 Vienna, Austria.
Martin Pabst
Laura Neumann
Michael J Coyne
Friedrich Altmann
Paul Messner
Laurie E Comstock
Christina Schäffer
BOKU University · ATHarvard University · US

Funding

Structural, genetic, and functional analyses of the glycoproteins of BacteroidesR01AI067711 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI COMSTOCK, LAURIE E · 2006 to 2009
$1.4M
Austrian Science Fund FWF P 20605Austrian Science Fund FWF P 24317Austrian Science Fund FWF W 1224NIAID NIH HHS R01 AI067711NIAID NIH HHS R01AI067711
6 · The paper itself

Abstract

While it is now evident that the two Bacteroidales species Bacteroides fragilis and Tannerella forsythia both have general O-glycosylation systems and share a common glycosylation sequon, the ability of these organisms to glycosylate a protein native to the other organism has not yet been demonstrated. Here, we report on the glycosylation of heterologous proteins between these two organisms. Using genetic tools previously developed for Bacteroides species, two B. fragilis model glycoproteins were expressed in the fastidious anaerobe T. forsythia and the attachment of the known T. forsythia O-glycan to these proteins was demonstrated by liquid chromatography electrospray ionization tandem mass spectrometry. Likewise, two predominant T. forsythia glycoproteins were expressed in B. fragilis and glycosylation with the B. fragilis O-glycan was confirmed. Purification of these proteins from B. fragilis allowed the preliminary characterization of the previously uncharacterized B. fragilis protein O-glycan. Based on mass spectrometric data, we show that the B. fragilis protein O-glycan is an oligosaccharide composed of nine sugar units. Compositional and structural similarities with the T. forsythia O-glycan suggest commonalities in their biosynthesis. These data demonstrate the feasibility of exploiting these organisms for the design of novel glycoproteins.

Indexed as

Bacterial ProteinsBacteroidesCarbohydrate SequenceGlycoproteinsGlycosylationMolecular Sequence DataOligosaccharidesPolysaccharidesBacterial ProteinsGlycoproteinsOligosaccharidesPolysaccharides

Identifiers

PMID23258847
PMCPMC3608352
OpenAlexW2125863307

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.