Evidence map›Paper›PMID 24994902›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Modification and periplasmic translocation of the biofilm exopolysaccharide poly-β-1,6-N-acetyl-D-glucosamine.

Dustin J Little, Grace Li, Christopher Ing, Benjamin R DiFrancesco, Natalie C Bamford, Howard Robinson, Mark Nitz, Régis Pomès, P Lynne Howell

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Article
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  5. Adaptive traits ofmBio · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. The Determination, Monitoring, Molecular Mechanisms and Formation of Biofilm in E. coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
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  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Dustin J LittleProgram in Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Toronto, ON, Canada M5G 1X8;Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8;
Grace LiProgram in Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Toronto, ON, Canada M5G 1X8;Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8;
Christopher IngProgram in Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Toronto, ON, Canada M5G 1X8;Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8;
Benjamin R DiFrancescoDepartment of Chemistry, University of Toronto, Toronto, ON, Canada M5S 3H6; and.
Natalie C BamfordProgram in Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Toronto, ON, Canada M5G 1X8;Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8;
Howard RobinsonPhoton Sciences Division, Brookhaven National Laboratory, Upton, NY 11973-5000.
Mark NitzDepartment of Chemistry, University of Toronto, Toronto, ON, Canada M5S 3H6; and howell@sickkids.ca mnitz@chem.utoronto.ca pomes@sickkids.ca.
Régis PomèsProgram in Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Toronto, ON, Canada M5G 1X8;Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8; howell@sickkids.ca mnitz@chem.utoronto.ca pomes@sickkids.ca.
P Lynne HowellProgram in Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Toronto, ON, Canada M5G 1X8;Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8; howell@sickkids.ca mnitz@chem.utoronto.ca pomes@sickkids.ca.

Funding

Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
CIHRNIGMS NIH HHS P41 GM111244
6 · The paper itself

Abstract

Poly-β-1,6-N-acetyl-D-glucosamine (PNAG) is an exopolysaccharide produced by a wide variety of medically important bacteria. Polyglucosamine subunit B (PgaB) is responsible for the de-N-acetylation of PNAG, a process required for polymer export and biofilm formation. PgaB is located in the periplasm and likely bridges the inner membrane synthesis and outer membrane export machinery. Here, we present structural, functional, and molecular simulation data that suggest PgaB associates with PNAG continuously during periplasmic transport. We show that the association of PgaB's N- and C-terminal domains forms a cleft required for the binding and de-N-acetylation of PNAG. Molecular dynamics (MD) simulations of PgaB show a binding preference for N-acetylglucosamine (GlcNAc) to the N-terminal domain and glucosammonium to the C-terminal domain. Continuous ligand binding density is observed that extends around PgaB from the N-terminal domain active site to an electronegative groove on the C-terminal domain that would allow for a processive mechanism. PgaB's C-terminal domain (PgaB310-672) directly binds PNAG oligomers with dissociation constants of ∼1-3 mM, and the structures of PgaB310-672 in complex with β-1,6-(GlcNAc)6, GlcNAc, and glucosamine reveal a unique binding mode suitable for interaction with de-N-acetylated PNAG (dPNAG). Furthermore, PgaB310-672 contains a β-hairpin loop (βHL) important for binding PNAG that was disordered in previous PgaB42-655 structures and is highly dynamic in the MD simulations. We propose that conformational changes in PgaB310-672 mediated by the βHL on binding of PNAG/dPNAG play an important role in the targeting of the polymer for export and its release.

Indexed as

BiofilmsAmidohydrolasesbeta-GlucansBiological Transport, ActiveEscherichia coliEscherichia coli ProteinsMolecular Docking SimulationPeriplasmPolysaccharides, BacterialProtein Structure, SecondaryProtein Structure, TertiaryAmidohydrolasesbeta-GlucansEscherichia coli Proteinspoly-beta-1,6-N-acetyl-D-glucosamine de-N-acetylase, E colipoly-N-acetyl-1-6-glucosaminePolysaccharides, Bacterialcarbohydrate bindingdeacetylaseexopolysaccharide biosynthesisglycobiology

Identifiers

PMID24994902
PMCPMC4121833

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.