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Related Experiment Videos

Streptococcus mutans binding to solid phase dextran mediated by the glucan-binding protein C.

Y Sato1, H Senpuku, K Okamoto

  • 1Department of Biochemistry, Tokyo Dental College, Masago 1-chome, Mihama-ku, Chiba City, Japan.

Oral Microbiology and Immunology
|July 18, 2002
PubMed
Summary

Streptococcus mutans GbpC protein, linked to stress-induced aggregation, was detected in cells exhibiting negative dextran-dependent aggregation. These cells could bind to dextran, revealing a novel role for GbpC.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Streptococcus mutans is a key pathogen in dental caries.
  • Cell wall-anchored surface proteins play crucial roles in bacterial adhesion and aggregation.
  • Dextran-dependent aggregation is a significant factor in S. mutans biofilm formation.

Purpose of the Study:

  • To detect and characterize the GbpC protein in Streptococcus mutans.
  • To investigate the role of GbpC in dextran-dependent aggregation under stress conditions.
  • To determine if GbpC expression correlates with the dextran-dependent aggregation (ddag) phenotype.

Main Methods:

  • Isolation of the cell wall fraction of S. mutans after N-acetylmuramidase digestion.
  • Western blot analysis using anti-GbpC serum to detect the GbpC protein.

Related Experiment Videos

  • Assessment of dextran-dependent aggregation (ddag) phenotype in S. mutans cells.

    • Main Results:

    • The GbpC protein was successfully detected in S. mutans.
    • GbpC expression was observed in cells exhibiting the negative dextran-dependent aggregation (ddag) phenotype.
    • S. mutans cells expressing GbpC demonstrated the ability to bind to immobilized dextran.

    Conclusions:

    • The GbpC protein is present in Streptococcus mutans and is associated with stress conditions.
    • GbpC expression is linked to the negative dextran-dependent aggregation (ddag) phenotype.
    • The GbpC protein facilitates the binding of S. mutans to dextran, suggesting a role in adhesion mechanisms.