Evidence map›Paper›PMID 23475978›Full record

ArticleJournal of bacteriology2013

Agl16, a thermophilic glycosyltransferase mediating the last step of N-Glycan biosynthesis in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius.

Benjamin H Meyer, Elham Peyfoon, Carsten Dietrich, Paul Hitchen, Maria Panico, Howard R Morris, Anne Dell, Sonja-Verena Albers

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Journal of bacteriology · 2026
    Review
  2. Article
  3. Article
  4. Membrane lipid and expression responses ofFrontiers in microbiology · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Identifying Components of aFrontiers in microbiology · 2021
    Article
  9. Identification of a novelThe Journal of biological chemistry · 2020
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. UDP-sulfoquinovose formation by Sulfolobus acidocaldarius.Extremophiles : life under extreme conditions · 2015
    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

8 authors at 2 institutions in 2 countries.

Benjamin H MeyerMolecular Biology of Archaea, Max-Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Elham Peyfoon
Carsten Dietrich
Paul Hitchen
Maria Panico
Howard R Morris
Anne Dell
Sonja-Verena Albers
Imperial College London · GBMax Planck Institute for Terrestrial Microbiology · DE

Funding

Biotechnology and Biological Sciences Research Council BBC5196701Biotechnology and Biological Sciences Research Council BBF0083091
6 · The paper itself

Abstract

Recently, the S-layer protein of Sulfolobus acidocaldarius was shown to be N-linked with a tribranched hexasaccharide, composed of Man2Glc1GlcNAc2 and a sulfated sugar called sulfoquinovose. To identify genes involved in the biosynthesis and attachment of this glycan, markerless in-frame deletions of genes coding for predicted glycosyltransferases were created. The successful deletion of agl16, coding for a glycosyltransferase, resulted in the S-layer protein and archaellins having reduced molecular weights, as visualized by Coomassie staining or immunoblotting. This analysis indicated a change in the N-glycan composition. Nano-liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses confirmed that the glycan of the S-layer protein from the agl16 deletion mutant was a pentasaccharide, which was missing a terminal hexose residue. High-performance liquid chromatography (HPLC) analyses of the hydrolyzed N-glycan indicated that the missing hexose is a glucose residue. A physiological characterization of the agl16 deletion mutant revealed a significant effect on the growth at elevated salt concentrations. At 300 mM NaCl, the doubling time of the Δagl16 mutant was increased 2-fold compared to that of the background strain. Furthermore, the incomplete glycan structure of the Δagl16 deletion strain affected the assembly and function of the archaellum, as exemplified by semisolid Gelrite plate analysis, in which the motility is decreased according to the N-glycan size.

Indexed as

Bacterial ProteinsChromatography, High Pressure LiquidChromatography, LiquidGlycosyltransferasesPolysaccharidesSulfolobus acidocaldariusTandem Mass SpectrometryBacterial ProteinsGlycosyltransferasesPolysaccharides

Identifiers

PMID23475978
PMCPMC3650533
OpenAlexW2108027570

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.