Evidence map›Paper›PMID 24118505›Full record

ArticleMolecular microbiology2013

O-linked protein glycosylation in Mycoplasma.

David S Jordan, James M Daubenspeck, Audra H Laube, Matthew B Renfrow, Kevin Dybvig

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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. 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

5 authors at 1 institution in 1 country.

David S JordanDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL, 35294, USA.
James M Daubenspeck
Audra H Laube
Matthew B Renfrow
Kevin Dybvig
University of Alabama at Birmingham · US

Funding

Mechanisms of Mycoplasmal Disease PathogenesisR01AI063909 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DYBVIG, KEVIN F · 2005 to 2014
$3.0M
Analytical tools for the analysis of clustered O-glycans in clinical samplesR01GM098539 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI RENFROW, MATTHEW B · 2011 to 2019
$2.7M
MECHANISMS OF MYCOPLASMA-INDUCED ARTHRITISR01AR044252 · NIAMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DYBVIG, KEVIN F · 1997 to 2009
$2.4M
Mycoplasma Polysaccharides and Control of InfectionR56AI093750 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DYBVIG, KEVIN F · 2012 to 2012
$366k
NIAID NIH HHS AI63909NIAID NIH HHS AI93750NIAID NIH HHS R01 AI063909NIAID NIH HHS R56 AI093750NIAMS NIH HHS AR44252NIAMS NIH HHS R01 AR044252NIGMS NIH HHS R01 GM098539
6 · The paper itself

Abstract

Although mycoplasmas have a paucity of glycosyltransferases and nucleotidyltransferases recognizable by bioinformatics, these bacteria are known to produce polysaccharides and glycolipids. We show here that mycoplasmas also produce glycoproteins and hence have glycomes more complex than previously realized. Proteins from several species of Mycoplasma reacted with a glycoprotein stain, and the murine pathogen Mycoplasma arthritidis was chosen for further study. The presence of M. arthritidis glycoproteins was confirmed by high-resolution mass spectrometry. O-linked glycosylation was clearly identified at both serine and threonine residues. No consensus amino acid sequence was evident for the glycosylation sites of the glycoproteins. A single hexose was identified as the O-linked modification, and glucose was inferred by (13) C-labelling to be the hexose at several of the glycosylation sites. This is the first study to conclusively identify sites of protein glycosylation in any of the mollicutes.

Indexed as

Amino Acid SequenceBacterial ProteinsGlycoproteinsGlycosylationGlycosyltransferasesMass SpectrometryMycoplasma arthritidisPeptide MappingPolysaccharides, BacterialProtein Processing, Post-TranslationalSerineThreonineBacterial ProteinsGlycoproteinsGlycosyltransferasesPolysaccharides, BacterialSerineThreonine

Identifiers

PMID24118505
PMCPMC3843974
OpenAlexW2128811941

What OpenQuestion holds

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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.