Evidence map›Paper›PMID 23551589›Full record

ArticleMolecular microbiology2013

Phylum-wide general protein O-glycosylation system of the Bacteroidetes.

Michael J Coyne, C Mark Fletcher, Maria Chatzidaki-Livanis, Gerald Posch, Christina Schaffer, Laurie E Comstock

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 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

42 citing papers in PubMed, 68 citations in OpenAlex.

  1. High-throughput analyses ofGut microbes · 2026
    Article
  2. 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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  3. Review
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  7. An outer membrane vesicle specific lipoprotein promotesCurrent research in microbial sciences · 2024
    Article
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  9. Characterization of theJournal of bacteriology · 2023
    Article
  10. Article
  11. Review
  12. Article
  13. Applied and environmental microbiology · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  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

6 authors at 3 institutions in 2 countries.

Michael J CoyneDivision of Infectious Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
C Mark Fletcher
Maria Chatzidaki-Livanis
Gerald Posch
Christina Schaffer
Laurie E Comstock
BOKU University · ATBrigham and Women's Hospital · USHarvard University · US

Funding

Significance of Bacteroides fragilis polysaccharide phase variationR01AI081843 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI COMSTOCK, LAURIE E · 2010 to 2014
$1.9M
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
NIAID NIH HHS R01 AI067711NIAID NIH HHS R01AI067711NIAID NIH HHS R01 AI081843NIAID NIH HHS R01AI081843
6 · The paper itself

Abstract

The human gut symbiont Bacteroides fragilis has a general protein O-glycosylation system in which numerous extracytoplasmic proteins are glycosylated at a three amino acid motif. In B. fragilis, protein glycosylation is a fundamental and essential property as mutants with protein glycosylation defects have impaired growth and are unable to competitively colonize the mammalian intestine. In this study, we analysed the phenotype of B. fragilis mutants with defective protein glycosylation and found that the glycan added to proteins is comprised of a core glycan and an outer glycan. The genetic region encoding proteins for the synthesis of the outer glycan is conserved within a Bacteroides species but divergent between species. Unlike the outer glycan, an antiserum raised to the core glycan reacted with all Bacteroidetes species tested, from all four classes of the phylum. We found that diverse Bacteroidetes species synthesize numerous glycoproteins and glycosylate proteins at the same three amino acid motif. The wide-spread conservation of this protein glycosylation system within the phylum suggests that this system of post-translational protein modification evolved early, before the divergence of the four classes of Bacteroidetes, and has been maintained due to its physiological importance to the diverse species of this phylum.

Indexed as

Bacterial ProteinsBacteroidetesConserved SequenceGenes, BacterialGlycoproteinsGlycosylationMetabolic Networks and PathwaysPolysaccharidesBacterial ProteinsGlycoproteinsPolysaccharides

Identifiers

PMID23551589
PMCPMC3656502
OpenAlexW2117317865

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.