Evidence map›Paper›PMID 22759313›Full record

ArticleMolecular oral microbiology2012

Effect of starch and amylase on the expression of amylase-binding protein A in Streptococcus gordonii.

A E Nikitkova, E M Haase, F A Scannapieco

Open access · greenAbstract read
In one paragraph

Article in Molecular oral microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.0field-weighted citation impact, top 11% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Observational
  4. Reply to Ben-Dor et al.: Oral bacteria of Neanderthals and modern humans exhibit evidence of starch adaptation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Microbial interactions in building of communities.Molecular oral microbiology · 2013
    Review
  9. Review
  10. 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 1 institution in 1 country.

A E NikitkovaDepartment of Oral Biology, School of Dental Medicine, University at Buffalo, State University of New York, Buffalo, NY 14214, USA.
E M Haase
F A Scannapieco
University at Buffalo, State University of New York · US

Funding

TRAINING PROGRAM IN PERIODONTAL DISEASEST32DE007034 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SCANNAPIECO, FRANK ANDREW · 1985 to 2008
$3.5M
AMYLASE BINDING STREPTOCOCCI, DENTAL PLAQUE AND CARIESR01DE009838 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SCANNAPIECO, FRANK ANDREW · 1998 to 2008
$2.6M
Amylase Binding Streptococci, Dental Plaque and CariesR56DE009838 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SCANNAPIECO, FRANK ANDREW · 2011 to 2011
$405k
SALIVARY AMYLASE AND DENTAL PLAQUE FORMATIONR29DE009838 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SCANNAPIECO, FRANK ANDREW · 1992 to 1996
–
TITANIUM ALLOYS FOR PARTIAL DENTURESR43DE007034 · NIDCR · GREENMARK, INC. · PI MARKER, BERNARD C · 1985 to 1985
–
NIDCR NIH HHS DE007034NIDCR NIH HHS DE09838NIDCR NIH HHS R01 DE009838NIDCR NIH HHS R56 DE009838NIDCR NIH HHS T32 DE007034
6 · The paper itself

Abstract

Streptococcus gordonii is a common oral commensal bacterial species in tooth biofilm (dental plaque) and specifically binds to salivary amylase through the surface exposed amylase-binding protein A (AbpA). When S. gordonii cells are pretreated with amylase, amylase bound to AbpA facilitates growth with starch as a primary nutrition source. The goal of this study was to explore possible regulatory effects of starch, starch metabolites and amylase on the expression of S. gordonii AbpA. An amylase ligand-binding assay was used to assess the expression of AbpA in culture supernatants and on bacterial cells from S. gordonii grown in defined medium supplemented with 1% starch, 0.5 mg ml(-1) amylase, with starch and amylase together, or with various linear malto-oligosaccharides. Transcription of abpA was determined by reverse transcription quantitative polymerase chain reaction. AbpA was not detectable in culture supernatants containing either starch alone or amylase alone. In contrast, the amount of AbpA was notably increased when starch and amylase were both present in the medium. The expression of abpA was significantly increased (P < 0.05) following 40 min of incubation in defined medium supplemented with starch and amylase. Similar results were obtained in the presence of maltose and other short-chain malto-oligosacchrides. These results suggest that the products of starch hydrolysis produced from the action of salivary α-amylase, particularly maltose and maltotriose, up-regulate AbpA expression in S. gordonii.

Indexed as

Gene Expression Regulation, EnzymologicAmylasesBacterial Outer Membrane ProteinsEnzyme InductionHumansHydrolysisMaltosePolysaccharidesSalivaStarchStreptococcus gordoniiAbpA protein, Streptococcus gordoniiAmylasesBacterial Outer Membrane ProteinsmaltodextrinMaltosePolysaccharidesStarch

Identifiers

PMID22759313
PMCPMC3390759
OpenAlexW1949563070

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Registered trials

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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.