Evidence map›Paper›PMID 23827139›Full record

ArticleJournal of molecular biology2013

Sum of the parts: composition and architecture of the bacterial extracellular matrix.

Oscar A McCrate, Xiaoxue Zhou, Courtney Reichhardt, Lynette Cegelski

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

74 citing papers in PubMed, 147 citations in OpenAlex.

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14 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

4 authors at 1 institution in 1 country.

Oscar A McCrateDepartment of Chemistry, Stanford University, Stanford, CA 94305, USA.
Xiaoxue Zhou
Courtney Reichhardt
Lynette Cegelski
Stanford University · US

Funding

Structure, Function, and Disruption of Microbial Amyloid Assembly and Biofilm ForDP2OD007488 · OD · STANFORD UNIVERSITY · PI CEGELSKI, LYNETTE S · 2010 to 2010
$2.4M
NIH HHS DP2 OD007488NIH HHS DP2OD007488
6 · The paper itself

Abstract

Bacterial biofilms are complex multicellular assemblies that exhibit resistance to antibiotics and contribute to the pathogenesis of serious and chronic infectious diseases. New approaches and quantitative data are needed to define the molecular composition of bacterial biofilms. Escherichia coli biofilms are known to contain polysaccharides and functional amyloid fibers termed curli, yet accurate determinations of biofilm composition at the molecular level have been elusive. The ability to define the composition of the extracellular matrix (ECM) is crucial for the elucidation of structure-function relationships that will aid the development of chemical strategies to disrupt biofilms. We have developed an approach that integrates non-perturbative preparation of the ECM with electron microscopy, biochemistry, and solid-state NMR spectroscopy to define the chemical composition of the intact and insoluble ECM of a clinically important pathogenic bacterium--uropathogenic E. coli. Our data permitted a sum-of-all-the-parts analysis. Electron microscopy revealed supramolecular shell-like structures that encapsulated single cells and enmeshed the bacterial community. Biochemical and solid-state NMR measurements of the matrix and constitutive parts established that the matrix is composed of two major components, curli and cellulose, each in a quantifiable amount. This approach to quantifying the matrix composition is widely applicable to other organisms and to examining the influence of biofilm inhibitors. Collectively, our NMR spectra and the electron micrographs of the purified ECM inspire us to consider the biofilm matrix not as an undefined slime, but as an assembly of polymers with a defined composition and architecture.

Indexed as

BiofilmsAmyloidBacteriaBacterial ProteinsCelluloseExtracellular MatrixPolysaccharidesAmyloidBacterial ProteinsCelluloseCrl protein, BacteriaPolysaccharidesbiofilmCPMAScross-polarization magic-angle spinningcurliECMextracellular matrixfunctional amyloidmagic-angle spinningMASNMRREDORrotational-echo double-resonance

Identifiers

PMID23827139
PMCPMC3812305
OpenAlexW2052908852

What OpenQuestion holds

Textmetadata
LicenceTDM
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.