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Distribution of WGA-binding sites on the surface of clinical isolates of Staphylococcus aureus

S Yamada1, A Matsumoto, K Uehira

  • 1Department of Microbiology, Kawasaki Medical School, Okayama, Japan.

Journal of Electron Microscopy
|June 1, 1994
PubMed

Insights

Wheat germ agglutinin (WGA) binding varied significantly on Staphylococcus aureus surfaces. Methicillin-sensitive S. aureus (MSSA) showed heavier labeling than methicillin-resistant S. aureus (MRSA), indicating diverse surface carbohydrate expression.

Area of Science:

  • Microbiology
  • Biochemistry
  • Cell Biology

Background:

  • Staphylococcus aureus is a significant human pathogen.
  • Understanding surface characteristics is crucial for differentiating strains.
  • Wheat germ agglutinin (WGA) binds to N-acetylglucosamine and sialic acid residues.

Purpose of the Study:

  • To investigate the distribution and quantity of WGA-binding sites on clinical isolates of Staphylococcus aureus.
  • To compare WGA binding between methicillin-sensitive S. aureus (MSSA) and methicillin-resistant S. aureus (MRSA).

Main Methods:

  • Utilized WGA-gold labeling for electron microscopy to visualize WGA-binding sites.
  • Employed an alkaline phosphatase-WGA assay to quantify WGA binding.
  • Examined clinical isolates of both MSSA and MRSA strains.

Main Results:

  • WGA-binding was consistently lower on MRSA isolates compared to MSSA isolates.
  • MSSA isolates exhibited considerable diversity in the extent of WGA binding.
  • WGA-gold labeling was heavier on MSSA strains than on MRSA strains.

Conclusions:

  • Significant variations exist in the distribution and quantity of WGA-binding carbohydrates on the surface of Staphylococcus aureus.
  • These findings suggest potential differences in cell surface composition between MSSA and MRSA.
  • Further research into these surface carbohydrate differences may reveal novel targets for therapeutic intervention.

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