F-type proton-pumping ATPase mediates acid tolerance in Streptococcus mutans.
Streptococcus mutans
ATP synthase
F-ATPase
acid tolerance
dental caries
proton-pumping atpase
Journal
Journal of applied microbiology
ISSN: 1365-2672
Titre abrégé: J Appl Microbiol
Pays: England
ID NLM: 9706280
Informations de publication
Date de publication:
03 Apr 2023
03 Apr 2023
Historique:
received:
23
12
2022
revised:
01
04
2023
accepted:
12
04
2023
medline:
19
4
2023
pubmed:
14
4
2023
entrez:
13
4
2023
Statut:
ppublish
Résumé
Streptococcus mutans is highly sensitive to inhibitors of proton-pumping F-type ATPase (F-ATPase) under acidic conditions. Herein, we investigated the role of S. mutans F-ATPase in acid tolerance using a bacterium expressing the F-ATPase β subunit at lower levels than the wild-type strain. We generated a mutant S. mutans expressing the catalytic β subunit of F-ATPase at lower levels than the wild-type bacterium. The mutant cells exhibited a significantly slower growth rate at pH 5.30, whereas the rate was essentially the same as that of wild-type cells at pH 7.40. In addition, the colony-forming ability of the mutant was decreased at pH <4.30 but not at pH 7.40. Thus, the growth rate and survival of S. mutans expressing low levels of the β subunit were reduced under acidic conditions. Together with our previous observations, this study indicates that F-ATPase is involved in the acid tolerance mechanism of S. mutans by secreting protons from the cytoplasm.
Identifiants
pubmed: 37055370
pii: 7117960
doi: 10.1093/jambio/lxad073
pii:
doi:
Substances chimiques
Adenosine Triphosphatases
EC 3.6.1.-
Proton Pumps
0
Protons
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Japan Society for the Promotion of Science
ID : JP18K06629
Organisme : Keiryokai Research Foundation
ID : 142
Informations de copyright
© The Author(s) 2023. Published by Oxford University Press on behalf of Applied Microbiology International.