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  • Title: [A comparison of the activities of membrane-bound, proton translocating ATPases between Streptococcus mutans fluoride-resistant and their parent strains].
    Author: Sheng JY, Huang ZW, Liu Z.
    Journal: Shanghai Kou Qiang Yi Xue; 2005 Feb; 14(1):71-3. PubMed ID: 15747020.
    Abstract:
    PURPOSE: To figure out the reason for increased acid tolerance of Ingbritt-FR, the fluoride-resistant strain of Streptococcus mutans Ingbritt, by determining and comparing the H(+)-ATPase activities of both fluoride-resistant and their parental strains. METHODS: The permeabilized cells of S. mutans Ingbritt and Ingbritt-FR were prepared by treating them with 10% toluene and then two cycles of freezing and thawing. The permeabilized cells were used for ATPase assay by adding them to the reaction mixture which contained 50mM Tris-maleate buffer (pH 6.0), 10 mM MgSO4 and 5 mM ATP. ATPase activity was assessed by measuring inorganic phosphate released from ATP hydrolysis.Two-way ANOVA was used for statistical analysis. RESULTS: The activities of H(+)-ATPase of Ingbritt-FR were 308.48, 136.67, and 82.80 micromol Pi/g cell dry weight/min, at 10, 20, and 60 minutes respectively, significantly higher than those of their parent strain: 104.77, 64.69, and 30.7 (P<0.01). The enzyme activities were decreasing with time. CONCLUSIONS: The higher ATPase activity of fluoride-resistant mutant of S. mutans Ingbritt may account for the increased acid tolerance of this organism, and the increment of ATPase activity and acid tolerance of fluoride-resistant strain is likely to increase the cariogenic potential of S. mutans after fluoride-resistant mutation.
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