Identification and functional analysis of glutamine transporter in Streptococcus mutans
Background Streptococcus mutans, a biofilm-forming bacterium, possesses several transporters that function as import/export molecules. Among them, the PII protein family is composed of members that regulate glutamine synthesis in bacterial species. Objective In this study, we characterized the funct...
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doaj-c9c50c54dde54e5d8a83b29a592bbb182021-06-02T08:43:38ZengTaylor & Francis GroupJournal of Oral Microbiology2000-22972020-01-0112110.1080/20002297.2020.17973201797320Identification and functional analysis of glutamine transporter in Streptococcus mutansYuko Morikawa0Setsuyo Morimoto1Eri Yoshida2Shuhei Naka3Hiroaki Inaba4Michiyo Matsumoto-Nakano5Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical SciencesOkayama University Graduate School of Medicine, Dentistry and Pharmaceutical SciencesOkayama University Graduate School of Medicine, Dentistry and Pharmaceutical SciencesOkayama University Graduate School of Medicine, Dentistry and Pharmaceutical SciencesOkayama University Graduate School of Medicine, Dentistry and Pharmaceutical SciencesOkayama University Graduate School of Medicine, Dentistry and Pharmaceutical SciencesBackground Streptococcus mutans, a biofilm-forming bacterium, possesses several transporters that function as import/export molecules. Among them, the PII protein family is composed of members that regulate glutamine synthesis in bacterial species. Objective In this study, we characterized the function of the glutamine transporter in S. mutans MT8148. Methods The SMU.732 gene, corresponding to glnP in S. mutans, is homologous to the glutamine transporter gene in Bacillus subtilis. We constructed a glnP-inactivated mutant strain (GEMR) and a complement strain (comp-GEMR) and evaluated their biological functions. Results Growth of GEMR was similar in the presence and absence of glutamine, whereas the growth rates of MT8148 and comp-GEMR were significantly lower in the presence of glutamine as compared to its absence. Furthermore, biofilms formed by MT8148 and comp-GEMR were significantly thicker than that formed by GEMR, while the GEMR strain showed a significantly lower survival rate in an acidic environment than the other strains. Addition of n-phenyl-2-naphthylamine, used to label of the membrane, led to increased fluorescence intensity of MT8148 and GEMR, albeit that was significantly lower in the latter. Conclusions These results suggest that glnP is associated with glutamine transport in S. mutans, especially the import of glutamine involved in biofilm formation.http://dx.doi.org/10.1080/20002297.2020.1797320streptococcus mutansglutamine transporterbiofilmmembrane proteinglnp |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yuko Morikawa Setsuyo Morimoto Eri Yoshida Shuhei Naka Hiroaki Inaba Michiyo Matsumoto-Nakano |
spellingShingle |
Yuko Morikawa Setsuyo Morimoto Eri Yoshida Shuhei Naka Hiroaki Inaba Michiyo Matsumoto-Nakano Identification and functional analysis of glutamine transporter in Streptococcus mutans Journal of Oral Microbiology streptococcus mutans glutamine transporter biofilm membrane protein glnp |
author_facet |
Yuko Morikawa Setsuyo Morimoto Eri Yoshida Shuhei Naka Hiroaki Inaba Michiyo Matsumoto-Nakano |
author_sort |
Yuko Morikawa |
title |
Identification and functional analysis of glutamine transporter in Streptococcus mutans |
title_short |
Identification and functional analysis of glutamine transporter in Streptococcus mutans |
title_full |
Identification and functional analysis of glutamine transporter in Streptococcus mutans |
title_fullStr |
Identification and functional analysis of glutamine transporter in Streptococcus mutans |
title_full_unstemmed |
Identification and functional analysis of glutamine transporter in Streptococcus mutans |
title_sort |
identification and functional analysis of glutamine transporter in streptococcus mutans |
publisher |
Taylor & Francis Group |
series |
Journal of Oral Microbiology |
issn |
2000-2297 |
publishDate |
2020-01-01 |
description |
Background Streptococcus mutans, a biofilm-forming bacterium, possesses several transporters that function as import/export molecules. Among them, the PII protein family is composed of members that regulate glutamine synthesis in bacterial species. Objective In this study, we characterized the function of the glutamine transporter in S. mutans MT8148. Methods The SMU.732 gene, corresponding to glnP in S. mutans, is homologous to the glutamine transporter gene in Bacillus subtilis. We constructed a glnP-inactivated mutant strain (GEMR) and a complement strain (comp-GEMR) and evaluated their biological functions. Results Growth of GEMR was similar in the presence and absence of glutamine, whereas the growth rates of MT8148 and comp-GEMR were significantly lower in the presence of glutamine as compared to its absence. Furthermore, biofilms formed by MT8148 and comp-GEMR were significantly thicker than that formed by GEMR, while the GEMR strain showed a significantly lower survival rate in an acidic environment than the other strains. Addition of n-phenyl-2-naphthylamine, used to label of the membrane, led to increased fluorescence intensity of MT8148 and GEMR, albeit that was significantly lower in the latter. Conclusions These results suggest that glnP is associated with glutamine transport in S. mutans, especially the import of glutamine involved in biofilm formation. |
topic |
streptococcus mutans glutamine transporter biofilm membrane protein glnp |
url |
http://dx.doi.org/10.1080/20002297.2020.1797320 |
work_keys_str_mv |
AT yukomorikawa identificationandfunctionalanalysisofglutaminetransporterinstreptococcusmutans AT setsuyomorimoto identificationandfunctionalanalysisofglutaminetransporterinstreptococcusmutans AT eriyoshida identificationandfunctionalanalysisofglutaminetransporterinstreptococcusmutans AT shuheinaka identificationandfunctionalanalysisofglutaminetransporterinstreptococcusmutans AT hiroakiinaba identificationandfunctionalanalysisofglutaminetransporterinstreptococcusmutans AT michiyomatsumotonakano identificationandfunctionalanalysisofglutaminetransporterinstreptococcusmutans |
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