Evidence map›Paper›PMID 26280561›Full record

ArticleMolecular oral microbiology2016

Surface display of Aggregatibacter actinomycetemcomitans autotransporter Aae and dispersin B hybrid act as antibiofilm agents.

C Ragunath, K DiFranco, M Shanmugam, P Gopal, V Vyas, D H Fine, C Cugini, N Ramasubbu

Open access · greenAbstract read
In one paragraph

Article in Molecular oral microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Pathogens (Basel, Switzerland) · 2024
    Review
  3. Article
  4. 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

8 authors at 1 institution in 1 country.

C RagunathDepartment of Oral Biology, Rutgers School of Dental Medicine, Newark, NJ, USA.
K DiFrancoDepartment of Oral Biology, Rutgers School of Dental Medicine, Newark, NJ, USA.
M ShanmugamDepartment of Oral Biology, Rutgers School of Dental Medicine, Newark, NJ, USA.
P GopalDepartment of Oral Biology, Rutgers School of Dental Medicine, Newark, NJ, USA.
V VyasDepartment of Oral Biology, Rutgers School of Dental Medicine, Newark, NJ, USA.
D H FineDepartment of Oral Biology, Rutgers School of Dental Medicine, Newark, NJ, USA.
C CuginiDepartment of Oral Biology, Rutgers School of Dental Medicine, Newark, NJ, USA.
N RamasubbuDepartment of Oral Biology, Rutgers School of Dental Medicine, Newark, NJ, USA.
Rutgers, The State University of New Jersey · US

Funding

Structure/function studies of biofilm agents from AaR01DE016291 · NIDCR · UNIV OF MED/DENT OF NJ-NJ DENTAL SCHOOL · PI RAMASUBBU, NARAYANAN · 2005 to 2007
$682k
Structure/function studies of biofilm agents from AaR56DE016291 · NIDCR · UNIV OF MED/DENT OF NJ-NJ DENTAL SCHOOL · PI RAMASUBBU, NARAYANAN · 2009 to 2009
$351k
NIDCR NIH HHS R01 DE016291NIDCR NIH HHS R56 DE016291
6 · The paper itself

Abstract

Among the various proteins expressed by the periodontopathogen Aggregatibacter actinomycetemcomitans, two proteins play important roles for survival in the oral cavity. The autotransporter Aae facilitates the attachment of the pathogen to oral epithelial cells, which act as a reservoir, while the biofilm-degrading glycoside hydrolase dispersin B facilitates the movement of daughter cells from the mature biofilm to a new site. The objective of this study was to use the potential of these two proteins to control biofilms. To this end, we generated a hybrid construct between the Aae C-terminal translocating domain and dispersin B, and mobilized it into Escherichia coli Rosetta (DE3) pLysS cells. Immunofluorescence analysis of the modified E. coli cells confirmed the presence of dispersin B on the surface. Further, the membrane localization of the displayed dispersin B was confirmed with Western blot analysis. The integrity of the E. coli cells displaying the dispersin B was confirmed through FACS analysis. The hydrolytic activity of the surface-displayed dispersin B was confirmed by using 4-methylumbelliferyl-β-d-glucopyranoside as the substrate. The detachment ability of the dispersin B surface-displaying E. coli cells was shown using Staphylococcus epidermidis and Actinobacillus pleuropneumoniae biofilms in a microtiter assay. We concluded that the Aae β-domain is sufficient to translocate foreign enzymes in the native folded form and that the method of Aae-mediated translocation of surface displayed enzymes might be useful for control of biofilms.

Indexed as

Bacterial AdhesionActinobacillus pleuropneumoniaeAggregatibacter actinomycetemcomitansBacterial ProteinsBiofilmsCell Surface Display TechniquesEscherichia coliFlow CytometryGlycoside HydrolasesRecombinant Fusion ProteinsStaphylococcus epidermidisType V Secretion SystemsBacterial Proteinsdispersin B, Actinobacillus actinomycetemcomitansGlycoside HydrolasesRecombinant Fusion ProteinsType V Secretion Systemsautotransporterbiofilmdispersin Boral pathogensurface display

Identifiers

PMID26280561
PMCPMC6118125
OpenAlexW2143809997

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.