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. 2007 Oct;45(4):398-404.
doi: 10.1111/j.1472-765X.2007.02203.x.

Systemic inactivation and phenotypic characterization of two-component systems in expression of Streptococcus mutans virulence properties

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Systemic inactivation and phenotypic characterization of two-component systems in expression of Streptococcus mutans virulence properties

C M Lévesque et al. Lett Appl Microbiol. 2007 Oct.

Abstract

Aim: To assess potential function of each two-component signal transduction system in the expression of Streptococcus mutans virulence properties. VSports手机版.

Methods and results: For each two-component system (TCS), the histidine kinase-encoding gene was inactivated by a polymerase chain reaction (PCR)-based deletion strategy and the effects of gene disruption on the cell's ability to form biofilms, become competent, and tolerate acid, osmotic, and oxidative stress conditions were tested. Our results demonstrated that none of the mutations were lethal for S. mutans. The TCS-2 (CiaRH) is involved in biofilm formation and tolerance to environmental stresses, the TCS-3 (ScnRK-like) participates in the survival of cells at acidic pH, and the TCS-9 affects the acid tolerance response and the process of streptococcal competence development V体育安卓版. .

Conclusions: Our results confirmed the physiological role of the TCS in S. mutans cellular function, in particular the SncRK-like TCS and TCS-9 as they may represent new regulatory systems than can be involved in S V体育ios版. mutans pathogenesis. .

Significance and impact of the study: Multiple TCS govern important biological parameters of S. mutans enabling its survival and persistence in the biofilm community VSports最新版本. .

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Figures

Figure 1
Figure 1
Growth kinetics of UA159 (unstressed ◆, stressed ■), SMHK2 (▲), SMHK3 (•), and SMHK9 (×). (a) THYE (pH 5·5); (b) THYE (pH 7·5) with 0·5 mmol l–1 of hydrogen peroxide; (c) THYE (pH 7·5) with 2% NaCl.
Figure 2
Figure 2
Scanning electron micrographs of Streptococcus mutans UA159 (a–c) and SMHK2 (d–f) biofilms. Magnifications, ×1000 (a and d), ×2500 (b and e), and ×5000 (c and f).

References

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