Int J Oral Biol.  2019 Dec;44(4):152-159. 10.11620/IJOB.2019.44.4.152.

Weissella cibaria CMU suppresses mgl gene expression and enzyme activity associated with bad breath

Affiliations
  • 1Institute of Biomaterial Implant, Department of Oral Anatomy, School of Dentistry, Wonkwang University, Iksan 54538, Republic of Korea.
  • 2Research Institute, OraPharm Inc, Seoul 04781, Republic of Korea. jieenkang@orapharm.com
  • 3Department of Food and Nutrition, Hanyang University, Seoul 04763, Republic of Korea.
  • 4School of Nursing, Kangwon National University, Chuncheon 24341, Republic of Korea.

Abstract

The oral care probiotic strain Weissella cibaria CMU (oraCMU) inhibits volatile sulphur compounds associated with halitosis, presumably by inhibiting the growth of associated oral pathogens. In the present study, we investigated whether oraCMU inhibits the production of these compounds by suppressing the expression of mgl. This gene encodes L-methionine-α-deamino-γ-mercaptomethane-lyase (METase) and is involved in the production of methyl mercaptan (CH₃SH) by Porphyromonas gingivalis. Therefore, we specifically investigated the effects of oraCMU on the growth, CH₃SH production, METase activity, and mgl expression of P. gingivalis. The minimum inhibitory concentrations of cell-free supernatant and secreted proteins from oraCMU were 125 mg/mL and 800 µg/mL, respectively. At sub-minimum inhibitory concentration levels, these metabolites inhibited CH₃SH production, but they also reduced P. gingivalis viability. Only heat-killed oraCMU decreased CH₃SH production without affecting P. gingivalis viability. Heat-killed oraCMU also inhibited METase activity toward L-methionine and mgl mRNA expression (p < 0.05). In summary, we demonstrated the inhibition of volatile sulphur compounds via the antimicrobial action of oraCMU and, for the first time, the inhibition of such compounds by heat-killed oraCMU, which occurred at the molecular level.

Keyword

Probiotics; Halitosis; Porphyromonas gingivalis; Methyl mercaptan; L-methionine-α-deamino-γ-mercaptomethanelyase
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