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Agglutination of Staphylococcus saprophyticus: a structural and cytochemical study
1Laboratory of Electron Microscopy, Kyoto Prefectural University of Medicine, Japan.
FEMS Microbiology Letters
|October 1, 1995
Summary
Wheat germ agglutinin binds to Staphylococcus saprophyticus, causing its agglutination. This interaction involves N-acetylglucosamine binding sites on both the bacteria and sheep red blood cells.
Area of Science:
- Microbiology
- Biochemistry
- Cell Biology
Background:
- Staphylococcus saprophyticus is a common cause of urinary tract infections.
- Wheat germ agglutinin (WGA) is a lectin that binds to N-acetylglucosamine residues.
Purpose of the Study:
- To investigate the mechanism of Staphylococcus saprophyticus agglutination by wheat germ agglutinin.
- To identify the binding sites involved in this interaction.
Main Methods:
- Agglutination assays using WGA, WGA-biotin, and GlcNAc-BSA with S. saprophyticus and sheep red blood cells.
- Electron microscopy to visualize agglutination structures.
- Cytochemical analysis to determine binding sites.
Main Results:
- S. saprophyticus was agglutinated by WGA, WGA-biotin, GlcNAc-BSA, and sheep red blood cells.
- Electron microscopy revealed filamentous/amorphous structures on S. saprophyticus during agglutination.
- Cytochemical analysis confirmed WGA binding sites on S. saprophyticus and N-acetylglucosamine binding sites on both S. saprophyticus and sheep red blood cells.
Conclusions:
- The agglutination of S. saprophyticus by WGA is mediated by N-acetylglucosamine residues.
- An interaction between WGA-bindable substances on S. saprophyticus and N-acetylglucosamine-bindable substances on sheep red blood cells likely occurs.