Evidence map›Paper›PMID 22081384›Full record

ArticleJournal of bacteriology2012

The major autolysin Acm2 from Lactobacillus plantarum undergoes cytoplasmic O-glycosylation.

Lasse Fredriksen, Geir Mathiesen, Anders Moen, Peter A Bron, Michiel Kleerebezem, Vincent G H Eijsink, Wolfgang Egge-Jacobsen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2012. 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
8.8field-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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Lipoteichoic Acid InhibitsFrontiers in microbiology · 2018
    Article
  11. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  18. Review
  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

7 authors at 4 institutions in 2 countries.

Lasse FredriksenDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Aas, Norway.
Geir Mathiesen
Anders Moen
Peter A Bron
Michiel Kleerebezem
Vincent G H Eijsink
Wolfgang Egge-Jacobsen
Norwegian University of Life Sciences · NOUniversity of Oslo · NONederlands Instituut Voor Zuivel Oonderzoek · NLWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The major autolysin Acm2 from the probiotic strain Lactobacillus plantarum WCFS1 contains high proportions of alanine, serine, and threonine in its N-terminal so-called AST domain. It has been suggested that this extracellular protein might be glycosylated, but this has not been experimentally verified. We used high-resolution liquid chromatography-tandem mass spectrometry (LC-MS/MS) to study the possible occurrence of glycans on peptides generated from lactobacillary surface proteins by protease treatment. This approach yielded five glycopeptides in various glycoforms, all derived from the AST domain of Acm2. All five glycopeptides contained the hydroxy-amino acids serine and threonine, suggesting that Acm2 is O-glycosylated. By using lectin blotting with succinylated wheat germ agglutinin, and by comparing the wild-type strain with an Acm2-negative derivative (NZ3557), we found that the attached N-acetylhexosamines are most likely N-acetylglucosamines (GlcNAc). NZ3557 was further used as a genetic background to express an Acm2 variant lacking its secretion signal, resulting in intracellular expression of Acm2. We show that this intracellular version of Acm2 is also glycosylated, indicating that the GlcNAc modification is an intracellular process.

Indexed as

Amino Acid SequenceBacterial ProteinsCytoplasmDNA, BacterialGene DeletionGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGlycopeptidesGlycosylationLactiplantibacillus plantarumMolecular Sequence DataN-Acetylmuramoyl-L-alanine AmidaseBacterial ProteinsDNA, BacterialGlycopeptidesN-Acetylmuramoyl-L-alanine Amidase

Identifiers

PMID22081384
PMCPMC3256669
OpenAlexW2133071824

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.