Evidence map›Paper›PMID 20185825›Full record

ArticleThe Journal of biological chemistry2010

Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM.

Guoqing Xia, Lisa Maier, Patricia Sanchez-Carballo, Min Li, Michael Otto, Otto Holst, Andreas Peschel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

84 citing papers in PubMed, 154 citations in OpenAlex.

  1. Trial
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  12. Mechanistic study on the susceptibility ofApplied and environmental microbiology · 2025
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  18. International journal of molecular sciences · 2024
    Article
  19. Article
  20. Cryo-EM analysis ofScience advances · 2024
    Article

24 more citing papers are in PubMed but not listed here.

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.

Guoqing XiaDivision of Cellular and Molecular Microbiology, Interfaculty Institute of Microbiology and Infection Medicine, University of Tübingen, Elfriede-Aulhorn-Strasse 6, D-72076 Tübingen, Germany.
Lisa Maier
Patricia Sanchez-Carballo
Min Li
Michael Otto
Otto Holst
Andreas Peschel
University of Tübingen · DEResearch Center Borstel - Leibniz Lung Center · DENational Institute of Allergy and Infectious Diseases · USNational Institutes of Health · US

Funding

Staphylococcal pathogenesisZIAAI000904 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI OTTO, MICHAEL · 2009 to 2025
$22.6M
Staphylococcus Epidermidis Biofilm FormationZ01AI000904 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI OTTO, MICHAEL J · 2002 to 2008
$2.5M
Intramural NIH HHS Z01 AI000904
6 · The paper itself

Abstract

Wall teichoic acid (WTA) glycopolymers are major constituents of cell envelopes in Staphylococcus aureus and related gram-positive bacteria with important roles in cell wall maintenance, susceptibility to antimicrobial molecules, biofilm formation, and host interaction. Most S. aureus strains express polyribitol phosphate WTA substituted with D-alanine and N-acetylglucosamine (GlcNAc). WTA sugar modifications are highly variable and have been implicated in bacteriophage susceptibility and immunogenicity, but the pathway and enzymes of staphylococcal WTA glycosylation have remained unknown. Revisiting the structure of S. aureus RN4220 WTA by NMR analysis revealed the presence of canonical polyribitol phosphate WTA bearing only alpha-linked GlcNAc substituents. A RN4220 transposon mutant resistant to WTA-dependent phages was identified and shown to produce altered WTA, which exhibited faster electrophoretic migration and lacked completely the WTA alpha-GlcNAc residues. Disruption of a gene of unknown function, renamed tarM, was responsible for this phenotype. Recombinant TarM was capable of glycosylating WTA in vitro in a UDP-GlcNAc-dependent manner, thereby confirming its WTA GlcNAc-transferase activity. Deletion of the last seven amino acids from the C terminus abolished the activity of TarM. tarM-related genes were found in the genomes of several WTA-producing bacteria, suggesting that TarM-mediated WTA glycosylation is a general pathway in gram-positive bacteria. Our study represents a basis for dissecting the biosynthesis and function of glycosylated WTA in S. aureus and other bacteria.

Indexed as

AcetylglucosamineAmino Acid SequenceBacterial ProteinsCell WallDNA Transposable ElementsGene Knockdown TechniquesGlycosylationGlycosyltransferasesMagnetic Resonance SpectroscopyMutationPolysaccharidesRecombinant ProteinsSequence DeletionStaphylococcus aureusTeichoic AcidsAcetylglucosamineBacterial ProteinsDNA Transposable ElementsGlycosyltransferasespolyribitol phosphatePolysaccharidesRecombinant ProteinsTeichoic Acids

Identifiers

PMID20185825
PMCPMC2859500
OpenAlexW1982662495

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.