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Related Experiment Videos

Multiple glucan-binding proteins of Streptococcus sobrinus

Y Ma1, M O Lassiter, J A Banas

  • 1Department of Microbiology and Immunology, Academic Health Center, University of Louisville, Kentucky 40292, USA.

Journal of Bacteriology
|March 1, 1996
PubMed
Summary

Streptococcus sobrinus produces multiple glucan-binding proteins. A specific 60-kDa protein is identified as crucial for glucan-dependent cellular aggregation in this oral bacterium.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Streptococcus sobrinus is an oral bacterium known to produce various proteins.
  • Glucan-binding proteins play roles in bacterial adhesion and aggregation.

Purpose of the Study:

  • To identify and characterize glucan-binding proteins in Streptococcus sobrinus.
  • To determine the specific protein responsible for glucan-dependent cellular aggregation.

Main Methods:

  • Affinity chromatography using Sephadex G-75.
  • Elution with alpha-1,6 glucan and guanidine hydrochloride.
  • Gel electrophoresis and amino acid analysis.
  • Isolation and characterization of Streptococcus sobrinus mutants.

Main Results:

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  • Wild-type Streptococcus sobrinus possesses multiple glucan-binding proteins (16-145 kDa).
  • Two mutants lacking high-molecular-weight glucan-dependent aggregation were identified.
  • These mutants were specifically devoid of a 60-kDa protein.
  • The 60-kDa protein was distinct from other glucan-binding proteins and likely acts as a lectin.

Conclusions:

  • Streptococcus sobrinus produces several alpha-1,6 glucan-binding proteins.
  • A 60-kDa protein is essential for glucan-dependent cellular aggregation.
  • This 60-kDa protein is likely the specific lectin involved in aggregation.