Proton-pumping F-ATPase plays an important role in Streptococcus mutans under acidic conditions.
ATP synthase
Curcumin
F-ATPase
Polyphenol
Proton pump
Streptococcus mutans
Journal
Archives of biochemistry and biophysics
ISSN: 1096-0384
Titre abrégé: Arch Biochem Biophys
Pays: United States
ID NLM: 0372430
Informations de publication
Date de publication:
15 05 2019
15 05 2019
Historique:
received:
19
11
2018
revised:
25
03
2019
accepted:
26
03
2019
pubmed:
2
4
2019
medline:
27
2
2020
entrez:
2
4
2019
Statut:
ppublish
Résumé
Streptococcus mutans, a bacterium mainly inhabiting the tooth surface, is a major pathogen of dental caries. The bacterium metabolizes sugars to produce acids, resulting in an acidic microenvironment in the dental plaque. Hence, S. mutans should possess a mechanism for surviving under acidic conditions. In the current study, we report the effects of inhibitors of Escherichia coli proton-pumping F-type ATPase (F-ATPase) on the activity of S. mutans enzyme, and the growth and survival of S. mutans under acidic conditions. Piceatannol, curcumin, and demethoxycurcumin strongly reduced the ATPase activity of S. mutans F-ATPase. Interestingly, these compounds inhibited the growth of S. mutans at pH 5.3 but not at pH 7.3. They also significantly reduced the colony-forming ability of S. mutans after incubation at pH 4.3, while showing essentially no effect at pH 7.3. These observations indicate that S. mutans is highly sensitive to F-ATPase inhibitors under acidic conditions and that F-ATPase plays an important role in acid tolerance of this bacterium.
Identifiants
pubmed: 30930283
pii: S0003-9861(18)30941-X
doi: 10.1016/j.abb.2019.03.014
pii:
doi:
Substances chimiques
Proton Pumps
0
Adenosine Triphosphatases
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
46-51Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.