Evidence map›Paper›PMID 27520322›Full record

ArticleAnalytical and bioanalytical chemistry2017

Towards an automated analysis of bacterial peptidoglycan structure.

Marshall Bern, Richard Beniston, Stéphane Mesnage

Open access · hybridAbstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  4. Article
  5. Chemical science · 2024
    Article
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  14. Synthesis and Application of Methyl N,O-Hydroxylamine Muramyl Peptides.Chembiochem : a European journal of chemical biology · 2019
    Article
  15. Article
  16. Article
  17. Review
  18. Lytic transglycosylases: concinnity in concision of the bacterial cell wall.Critical reviews in biochemistry and molecular biology · 2017
    Review
  19. Review
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

3 authors at 2 institutions in 2 countries.

Marshall BernProtein Metrics Inc., 1622 San Carlos Ave., Suite C, San Carlos, CA, 94070, USA. bern@proteinmetrics.com.
Richard BenistonBiological Mass Spectrometry Facility biOMICS, University of Sheffield, Brook Hill Road, Sheffield, S3 7HF, UK.
Stéphane MesnageDepartment of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield, S10 2TN, UK. s.mesnage@sheffield.ac.uk.
University of Sheffield · GBProtein Metrics (United States) · US

Funding

Byologic: Software for Mass Spectrometric Protein Drug AssaysR44GM100634 · NIGMS · PROTEIN METRICS, LLC · PI KIL, YONG JOO · 2015 to 2016
$966k
Byologic: Software for Mass Spectrometric Protein Drug AssaysR43GM100634 · NIGMS · PROTEIN METRICS, LLC · PI KIL, YONG JOO · 2012 to 2012
$189k
Medical Research Council G1100127Medical Research Council MR/N002679/1NIGMS NIH HHS R43 GM100634NIGMS NIH HHS R44 GM100634
6 · The paper itself

Abstract

Peptidoglycan (PG) is an essential component of the bacterial cell envelope. This macromolecule consists of glycan chains alternating N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides containing nonstandard amino acids. Structural analysis of PG usually involves enzymatic digestion of glycan strands and separation of disaccharide peptides by reversed-phase HPLC followed by collection of individual peaks for MALDI-TOF and/or tandem mass spectrometry. Here, we report a novel strategy using shotgun proteomics techniques for a systematic and unbiased structural analysis of PG using high-resolution mass spectrometry and automated analysis of HCD and ETD fragmentation spectra with the Byonic software. Using the PG of the nosocomial pathogen Clostridium difficile as a proof of concept, we show that this high-throughput approach allows the identification of all PG monomers and dimers previously described, leaving only disambiguation of 3-3 and 4-3 cross-linking as a manual step. Our analysis confirms previous findings that C. difficile peptidoglycans include mainly deacetylated N-acetylglucosamine residues and 3-3 cross-links. The analysis also revealed a number of low abundance muropeptides with peptide sequences not previously reported. Graphical Abstract The bacterial cell envelope includes plasma membrane, peptidoglycan, and surface layer. Peptidoglycan is unique to bacteria and the target of the most important antibiotics; here it is analyzed by mass spectrometry.

Indexed as

AutomationBacterial ProteinsChemistry Techniques, AnalyticalPeptidoglycanSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationBacterial ProteinsPeptidoglycanCell wallCross-linkGlycoproteomicsMuropeptidesPeptidoglycanProteomicsTandem mass spectrometry

Identifiers

PMID27520322
PMCPMC5203844
OpenAlexW2516357724

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.