Evidence map›Paper›PMID 26599081›Full record

ArticlePloS one2015

General N-and O-Linked Glycosylation of Lipoproteins in Mycoplasmas and Role of Exogenous Oligosaccharide.

James M Daubenspeck, David S Jordan, Warren Simmons, Matthew B Renfrow, Kevin Dybvig

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Interaction between alveolar macrophages and epithelial cells duringFrontiers in cellular and infection microbiology · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. 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.

James M DaubenspeckDepartment of Genetics, University of Alabama at Birmingham, Birmingham, Alabama, United States of America.
David S JordanDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, United States of America.
Warren SimmonsDepartment of Genetics, University of Alabama at Birmingham, Birmingham, Alabama, United States of America.
Matthew B RenfrowDepartment of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, United States of America.
Kevin DybvigDepartment of Genetics, University of Alabama at Birmingham, Birmingham, Alabama, United States of America.
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
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 AI093750
6 · The paper itself

Abstract

The lack of a cell wall, flagella, fimbria, and other extracellular appendages and the possession of only a single membrane render the mycoplasmas structurally simplistic and ideal model organisms for the study of glycoconjugates. Most species have genomes of about 800 kb and code for few proteins predicted to have a role in glycobiology. The murine pathogens Mycoplasma arthritidis and Mycoplasma pulmonis have only a single gene annotated as coding for a glycosyltransferase but synthesize glycolipid, polysaccharide and glycoproteins. Previously, it was shown that M. arthritidis glycosylated surface lipoproteins through O-linkage. In the current study, O-linked glycoproteins were similarly found in M. pulmonis and both species of mycoplasma were found to also possess N-linked glycans at residues of asparagine and glutamine. Protein glycosylation occurred at numerous sites on surface-exposed lipoproteins with no apparent amino acid sequence specificity. The lipoproteins of Mycoplasma pneumoniae also are glycosylated. Glycosylation was dependent on the glycosidic linkages from host oligosaccharides. As far as we are aware, N-linked glycoproteins have not been previously described in Gram-positive bacteria, the organisms to which the mycoplasmas are phylogenetically related. The findings indicate that the mycoplasma cell surface is heavily glycosylated with implications for the modulation of mycoplasma-host interactions.

Indexed as

Amino Acid SequenceAsparagineBacterial ProteinsCell MembraneCell WallChromatography, GasChromatography, LiquidDisaccharidesElectrophoresis, Polyacrylamide GelGlutamineGlycoproteinsGlycosylationGram-Positive BacteriaHexosesLipoproteinsMass SpectrometryAsparagineBacterial ProteinsDisaccharidesGlutamineGlycoproteinsHexosesLipoproteinsOligosaccharides

Identifiers

PMID26599081
PMCPMC4657876
OpenAlexW2284499312

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.