Evidence map›Paper›PMID 24914184›Full record

ArticleJournal of bacteriology2014

GneZ, a UDP-GlcNAc 2-epimerase, is required for S-layer assembly and vegetative growth of Bacillus anthracis.

Ya-Ting Wang, Dominique Missiakas, Olaf Schneewind

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. ACS omega · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

3 authors at 2 institutions in 1 country.

Ya-Ting WangHoward Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA, and Department of Microbiology, University of Chicago, Chicago, Illinois, USA.
Dominique MissiakasHoward Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA, and Department of Microbiology, University of Chicago, Chicago, Illinois, USA.
Olaf SchneewindHoward Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA, and Department of Microbiology, University of Chicago, Chicago, Illinois, USA oschnee@bsd.uchicago.edu.
Argonne National Laboratory · USUniversity of Chicago · US

Funding

Vaccines and Therapies Against BotulismU54AI057153 · NIAID · UNIVERSITY OF CHICAGO · PI SHUMAN, HOWARD A · 2003 to 2013
$87.6M
Re-Engineering Translational Research at the University of ChicagoUL1TR000430 · NCATS · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2012 to 2016
$20.2M
Surface Proteins of Bacillus anthracisR01AI069227 · NIAID · UNIVERSITY OF CHICAGO · PI Dominique Missiakas · 2007 to 2026
$6.5M
Surface Proteins of Bacillus anthracisR37AI069227 · NIAID · UNIVERSITY OF CHICAGO · PI SCHNEEWIND, OLAF · 2017 to 2018
$809k
NCATS NIH HHS UL1 TR000430NIAID NIH HHS 1-U54-AI-057153NIAID NIH HHS AI069227NIAID NIH HHS R01 AI069227NIAID NIH HHS R37 AI069227NIAID NIH HHS U54 AI057153
6 · The paper itself

Abstract

Bacillus anthracis, the causative agent of anthrax, forms an S-layer atop its peptidoglycan envelope and displays S-layer proteins and Bacillus S-layer-associated (BSL) proteins with specific functions to support cell separation of vegetative bacilli and growth in infected mammalian hosts. S-layer and BSL proteins bind via the S-layer homology (SLH) domain to the pyruvylated secondary cell wall polysaccharide (SCWP) with the repeat structure [→4)-β-ManNAc-(1→4)-β-GlcNAc-(1→6)-α-GlcNAc-(1→]n, where α-GlcNAc and β-GlcNAc are substituted with two and one galactosyl residues, respectively. B. anthracis gneY (BAS5048) and gneZ (BAS5117) encode nearly identical UDP-GlcNAc 2-epimerase enzymes that catalyze the reversible conversion of UDP-GlcNAc and UDP-ManNAc. UDP-GlcNAc 2-epimerase enzymes have been shown to be required for the attachment of the phage lysin PlyG with the bacterial envelope and for bacterial growth. Here, we asked whether gneY and gneZ are required for the synthesis of the pyruvylated SCWP and for S-layer assembly. We show that gneZ, but not gneY, is required for B. anthracis vegetative growth, rod cell shape, S-layer assembly, and synthesis of pyruvylated SCWP. Nevertheless, inducible expression of gneY alleviated all the defects associated with the gneZ mutant. In contrast to vegetative growth, neither germination of B. anthracis spores nor the formation of spores in mother cells required UDP-GlcNAc 2-epimerase activity.

Indexed as

Bacillus anthracisCarbohydrate EpimerasesGene DeletionGenetic Complementation TestMembrane GlycoproteinsPolysaccharides, BacterialProtein MultimerizationCarbohydrate EpimerasesMembrane GlycoproteinsPolysaccharides, BacterialS-layer proteinsUDP acetylglucosamine-2-epimerase

Identifiers

PMID24914184
PMCPMC4135639
OpenAlexW2122447456

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.