Related Experiment Video
Updated: Aug 13, 2026

12:06
Generation of a Gene-disrupted Streptococcus mutans Strain Without Gene Cloning
Published on: October 23, 2017
[Streptococcus mutans glucosyltransferase: isolation and its ability to synthesize polysaccharides]
Summary
Extracellular glucosyltransferases (GTF) from Streptococcus mutans synthesize both water-soluble and insoluble glucans. Enzyme activity varied between serotypes, with serotype c strains showing a greater capacity for water-soluble glucan synthesis.
Area of Science:
- Microbiology
- Enzymology
- Biochemistry
Context:
- Streptococcus mutans is a primary etiological agent of dental caries.
- Extracellular glucosyltransferases (GTF) produced by S. mutans are key virulence factors.
- GTFs synthesize glucans from sucrose, contributing to biofilm formation and adherence.
Purpose:
- To characterize extracellular glucosyltransferases (GTF) from different strains of Streptococcus mutans.
- To compare the glucan synthesis capabilities of GTFs from S. mutans serotype g and serotype c.
- To investigate the complexity and enzymatic activity of S. mutans GTFs.
Summary:
- Extracellular glucosyltransferases (GTF) were successfully extracted from S. mutans strains (serotypes g and c) using ammonium sulfate precipitation with over 50% yield.
- All extracted enzyme preparations demonstrated the ability to synthesize both water-soluble and water-insoluble glucans.
- Polyacrylamide gel electrophoresis revealed the complex, multi-component nature of S. mutans GTFs. Significant differences in polysaccharide synthesis were observed between serotypes: GTFs from serotype g strains produced similar amounts of water-soluble and insoluble glucans, while GTFs from serotype c strains synthesized approximately 10 times more water-soluble glucan than water-insoluble glucan. No fructosyltransferase activity was detected.
Impact:
- Provides insights into the biochemical diversity of GTFs among different S. mutans serotypes.
- Highlights strain-specific differences in glucan synthesis, potentially influencing cariogenic potential.
- Contributes to understanding the enzymatic mechanisms underlying S. mutans virulence and biofilm formation.
Related Concept Videos
Oligosaccharide Assembly
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
Biosynthesis of Polysaccharides
Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
Peptidoglycan Synthesis
Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan biosynthesis begins in...

