Role of protease maturation lipoprotein in osmoadaptation of Streptococcus mutans. Issue 1 (26th June 2014)
- Record Type:
- Journal Article
- Title:
- Role of protease maturation lipoprotein in osmoadaptation of Streptococcus mutans. Issue 1 (26th June 2014)
- Main Title:
- Role of protease maturation lipoprotein in osmoadaptation of Streptococcus mutans
- Authors:
- Kunii, Maiko
Arimoto, Takafumi
Hasegawa, Tokuji
Kuwata, Hirotaka
Igarashi, Takeshi - Abstract:
- <abstract abstract-type="main" id="fml12477-abs-0001"> <title>Abstract</title> <p>Osmoadaptation may be an important trait for the pathogenicity of <italic>Streptococcus mutans</italic>. However, how this organism adapts to changes in osmolality in the oral cavity remains unclear. In this study, we showed that <italic>S. mutans</italic> utilizes K<sup>+</sup> for osmoadaptation, in which protease maturation lipoprotein (PrtM) plays an important role. Although growth of the wild‐type strain was impaired in a hyperosmotic medium [brain heart infusion (BHI) containing 0.3 M NaCl] compared with that in an unmodified BHI, the <italic>prtM</italic> mutant grew much more poorly in 0.3 M NaCl BHI. Comparison of growth behavior in the hyperosmotic medium supplemented with different osmoprotectants revealed that only the addition of K<sup>+</sup> allowed the bacteria to overcome the impairment of growth caused by the high osmolality. These results suggest that K<sup>+</sup> is an important compatible solute for <italic>S. mutans</italic>. Moreover, K<sup>+</sup>‐associated recovery of growth was not observed for the <italic>prtM</italic> mutant, indicating that PrtM plays a critical role in the utilization of K<sup>+</sup>. Quantitative reverse‐transcriptase polymerase chain reaction analysis showed that <italic>prtM</italic> was induced by osmotic stress, implying that <italic>prtM</italic> is an osmoresponsive gene. These findings suggest that K<sup>+</sup> is an important<abstract abstract-type="main" id="fml12477-abs-0001"> <title>Abstract</title> <p>Osmoadaptation may be an important trait for the pathogenicity of <italic>Streptococcus mutans</italic>. However, how this organism adapts to changes in osmolality in the oral cavity remains unclear. In this study, we showed that <italic>S. mutans</italic> utilizes K<sup>+</sup> for osmoadaptation, in which protease maturation lipoprotein (PrtM) plays an important role. Although growth of the wild‐type strain was impaired in a hyperosmotic medium [brain heart infusion (BHI) containing 0.3 M NaCl] compared with that in an unmodified BHI, the <italic>prtM</italic> mutant grew much more poorly in 0.3 M NaCl BHI. Comparison of growth behavior in the hyperosmotic medium supplemented with different osmoprotectants revealed that only the addition of K<sup>+</sup> allowed the bacteria to overcome the impairment of growth caused by the high osmolality. These results suggest that K<sup>+</sup> is an important compatible solute for <italic>S. mutans</italic>. Moreover, K<sup>+</sup>‐associated recovery of growth was not observed for the <italic>prtM</italic> mutant, indicating that PrtM plays a critical role in the utilization of K<sup>+</sup>. Quantitative reverse‐transcriptase polymerase chain reaction analysis showed that <italic>prtM</italic> was induced by osmotic stress, implying that <italic>prtM</italic> is an osmoresponsive gene. These findings suggest that K<sup>+</sup> is an important compatible solute for <italic>S. mutans</italic>, and that the osmoresponsive lipoprotein PrtM is involved in K<sup>+</sup> utilization, contributing to osmoadaptation of <italic>S. mutans</italic>.</p> </abstract> … (more)
- Is Part Of:
- FEMS microbiology letters. Volume 356:Issue 1(2014:Jul.)
- Journal:
- FEMS microbiology letters
- Issue:
- Volume 356:Issue 1(2014:Jul.)
- Issue Display:
- Volume 356, Issue 1 (2014)
- Year:
- 2014
- Volume:
- 356
- Issue:
- 1
- Issue Sort Value:
- 2014-0356-0001-0000
- Page Start:
- 45
- Page End:
- 52
- Publication Date:
- 2014-06-26
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1574-6968/issues ↗
http://www.sciencedirect.com/science/journal/03781097 ↗
http://onlinelibrary.wiley.com/ ↗
http://femsle.oxfordjournals.org/content/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1111/1574-6968.12477 ↗
- Languages:
- English
- ISSNs:
- 0378-1097
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.300000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4188.xml