Evidence map›Paper›PMID 34341504›Full record

ArticleThe ISME journal2022

A general approach to explore prokaryotic protein glycosylation reveals the unique surface layer modulation of an anammox bacterium.

Martin Pabst, Denis S Grouzdev, Christopher E Lawson, Hugo B C Kleikamp, Carol de Ram, Rogier Louwen, Yue Mei Lin, Sebastian Lücker, Mark C M van Loosdrecht, Michele Laureni

Open access · bronzeAbstract read
In one paragraph

Article in The ISME journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Exploring proteinmBio · 2025
    Article
  5. Review
  6. Journal of bacteriology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Membrane proteome of the thermoalkaliphileFrontiers in microbiology · 2023
    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

10 authors at 4 institutions in 2 countries.

Martin PabstDelft University of Technology, Department of Biotechnology, Delft, The Netherlands. m.pabst@tudelft.nl.ORCID http://orcid.org/0000-0001-9897-0723
Denis S GrouzdevSciBear OU, Tallinn, Estonia.ORCID http://orcid.org/0000-0002-1358-5146
Christopher E LawsonDOE Joint BioEnergy Institute, Lawrence Berkeley National Laboratory, Emeryville, CA, USA.
Hugo B C KleikampDelft University of Technology, Department of Biotechnology, Delft, The Netherlands.
Carol de RamDelft University of Technology, Department of Biotechnology, Delft, The Netherlands.
Rogier LouwenDepartment of Medical Microbiology and Infectious Diseases, Erasmus MC, University Medical Center Rotterdam, Rotterdam, The Netherlands.
Yue Mei LinDelft University of Technology, Department of Biotechnology, Delft, The Netherlands.
Sebastian LückerDepartment of Microbiology, IWWR, Radboud University, Nijmegen, the Netherlands.ORCID http://orcid.org/0000-0003-2935-4454
Mark C M van LoosdrechtDelft University of Technology, Department of Biotechnology, Delft, The Netherlands.ORCID http://orcid.org/0000-0003-0658-4775
Michele LaureniDelft University of Technology, Department of Biotechnology, Delft, The Netherlands.ORCID http://orcid.org/0000-0001-6248-8679
Delft University of Technology · NLErasmus MC · NLLawrence Berkeley National Laboratory · USRadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enormous chemical diversity and strain variability of prokaryotic protein glycosylation makes their large-scale exploration exceptionally challenging. Therefore, despite the universal relevance of protein glycosylation across all domains of life, the understanding of their biological significance and the evolutionary forces shaping oligosaccharide structures remains highly limited. Here, we report on a newly established mass binning glycoproteomics approach that establishes the chemical identity of the carbohydrate components and performs untargeted exploration of prokaryotic oligosaccharides from large-scale proteomics data directly. We demonstrate our approach by exploring an enrichment culture of the globally relevant anaerobic ammonium-oxidizing bacterium Ca. Kuenenia stuttgartiensis. By doing so we resolve a remarkable array of oligosaccharides, which are produced by two seemingly unrelated biosynthetic routes, and which modify the same surface-layer protein simultaneously. More intriguingly, the investigated strain also accomplished modulation of highly specialized sugars, supposedly in response to its energy metabolism-the anaerobic oxidation of ammonium-which depends on the acquisition of substrates of opposite charges. Ultimately, we provide a systematic approach for the compositional exploration of prokaryotic protein glycosylation, and reveal a remarkable example for the evolution of complex oligosaccharides in bacteria.

Indexed as

Ammonium CompoundsAnaerobic Ammonia OxidationAnaerobiosisBacteriaGlycosylationOxidation-ReductionAmmonium Compounds

Identifiers

PMID34341504
PMCPMC8776859
OpenAlexW3191556534

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.