Evidence map›Paper›PMID 26078454›Full record

ArticleThe Journal of biological chemistry2015

Identification of Poly-N-acetylglucosamine as a Major Polysaccharide Component of the Bacillus subtilis Biofilm Matrix.

Damien Roux, Colette Cywes-Bentley, Yi-Fan Zhang, Stephanie Pons, Melissa Konkol, Daniel B Kearns, Dustin J Little, P Lynne Howell, David Skurnik, Gerald B Pier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 114 citations in OpenAlex.

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  14. Biology and Regulation of Staphylococcal Biofilm.International journal of molecular sciences · 2023
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  15. Defining Early Steps inbioRxiv : the preprint server for biology · 2023
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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

10 authors at 4 institutions in 2 countries.

Damien RouxFrom the Division of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, and.
Colette Cywes-BentleyFrom the Division of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, and.
Yi-Fan ZhangFrom the Division of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, and Harvard School of Dental Medicine, Boston, Massachusetts 02115.
Stephanie PonsFrom the Division of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, and.
Melissa Konkolthe Department of Biology, Indiana University, Bloomington, Indiana 47405.
Daniel B Kearnsthe Department of Biology, Indiana University, Bloomington, Indiana 47405.
Dustin J Littlethe Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada, and the Program in Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada.
P Lynne Howellthe Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada, and the Program in Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada.
David SkurnikFrom the Division of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, and dskurnik@rics.bwh.harvard.edu.
Gerald B PierFrom the Division of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, and gpier@rics.bwh.harvard.edu.
Harvard University · USBrigham and Women's Hospital · USHospital for Sick Children · CAIndiana University Bloomington · US

Funding

Treatments for Nipah Virus InfectionU54AI057159 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI KASPER, DENNIS L. · 2003 to 2013
$113.7M
Pathogensis of Bacterial corneal infectionR01EY016144 · NEI · BRIGHAM AND WOMEN'S HOSPITAL · PI PIER, GERALD B · 2005 to 2018
$5.6M
The mechanism of bistable motility gene expression in Bacillus subtilis.R01GM093030 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI KEARNS, DANIEL B · 2010 to 2018
$2.6M
Canadian Institutes of Health Research 43998NEI NIH HHS EY016104NEI NIH HHS R01 EY016144NIAID NIH HHS AI057159NIAID NIH HHS U54 AI057159NIGMS NIH HHS GM093030NIGMS NIH HHS R01 GM093030PHS HHS U54A1057159
6 · The paper itself

Abstract

Bacillus subtilis is intensively studied as a model organism for the development of bacterial biofilms or pellicles. A key component is currently undefined exopolysaccharides produced from proteins encoded by genes within the eps locus. Within this locus are four genes, epsHIJK, known to be essential for pellicle formation. We show they encode proteins synthesizing the broadly expressed microbial carbohydrate poly-N-acetylglucosamine (PNAG). PNAG was present in both pellicle and planktonic wild-type B. subtilis cells and in strains with deletions in the epsA-G and -L-O genes but not in strains deleted for epsH-K. Cloning of the B. subtilis epsH-K genes into Escherichia coli with in-frame deletions in the PNAG biosynthetic genes pgaA-D, respectively, restored PNAG production in E. coli. Cloning the entire B. subtilis epsHIJK locus into pga-deleted E. coli, Klebsiella pneumoniae, or alginate-negative Pseudomonas aeruginosa restored or conferred PNAG production. Bioinformatic and structural predictions of the EpsHIJK proteins suggest EpsH and EpsJ are glycosyltransferases (GT) with a GT-A fold; EpsI is a GT with a GT-B fold, and EpsK is an α-helical membrane transporter. B. subtilis, E. coli, and pga-deleted E. coli carrying the epsHIJK genes on a plasmid were all susceptible to opsonic killing by antibodies to PNAG. The immunochemical and genetic data identify the genes and proteins used by B. subtilis to produce PNAG as a significant carbohydrate factor essential for pellicle formation.

Indexed as

BiofilmsAcetylglucosamineAntibodies, BacterialBacillus subtilisBacterial ProteinsBiosynthetic PathwaysEscherichia coliHL-60 CellsHumansModels, MolecularOpsonin ProteinsPhagocytosisPolysaccharides, BacterialProtein Structure, TertiaryAcetylglucosamineAntibodies, BacterialBacterial ProteinsOpsonin Proteinspoly-N-acetyl glucosaminePolysaccharides, Bacterialbacteriabacterial adhesionbacterial geneticscarbohydrate biosynthesiscarbohydrate structureglycobiologyglycosyltransferaseprotein expressionprotein structure

Identifiers

PMID26078454
PMCPMC4521046
OpenAlexW1562821755

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.