Related Experiment Videos
Functional analysis of glucan binding protein B from Streptococcus mutans.
Renata O Mattos-Graner1, Kristen A Porter, Daniel J Smith
1Department of Molecular Genetics, The Forsyth Institute, 140 Fenway, Boston, MA 02115, USA.
Journal of Bacteriology
|May 19, 2006
Summary
Streptococcus mutans glucan binding protein B (GbpB) is essential for bacterial survival, likely involved in cell division and peptidoglycan synthesis. Its gene expression is stress-inducible and strain-dependent.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Mutans streptococci are key causes of dental caries.
- Secreted bacterial products, like glucan binding protein B (GbpB), aid tooth colonization.
- GbpB's function is unknown, but homology suggests a role in murein biosynthesis.
Purpose of the Study:
- To elucidate the cellular function of Streptococcus mutans GbpB.
- To investigate GbpB gene essentiality and expression patterns.
- To identify proteins interacting with GbpB.
Main Methods:
- Gene inactivation attempts via transformation.
- Analysis of gene expression using Northern blot and real-time PCR.
- Protein interaction studies using pull-down and coimmunoprecipitation assays.
Main Results:
- Complete inactivation of the gbpB gene was unsuccessful, indicating it is essential.
- GbpB expression is stress-inducible in a strain-dependent manner.
- GbpB interacts with ribosomal protein L7/L12, suggesting a role in peptidoglycan synthesis and cell division.
Conclusions:
- Streptococcus mutans GbpB is an essential gene.
- GbpB is likely involved in peptidoglycan synthesis and cell division.
- GbpB interacts with ribosomal protein L7/L12, forming a complex potentially regulating these processes.