Agglutination of Staphylococcus saprophyticus: a structural and cytochemical study.

Staphylococcus saprophyticus was shown to be agglutinated by wheat germ agglutinin, wheat germ agglutinin-biotin and bovine serum albumin-p-aminophenyl-N-acetyl-beta-D-glucosaminide (GlcNAc-BSA), and sheep red blood cells. In these agglutinations, filamentous or amorphous structures radiating from the surface of S. saprophyticus were demonstrated by electron microscope observation. Cytochemical analyses of the agglutination revealed the binding sites of wheat germ agglutinin in S. saprophyticus and the binding sites of GlcNAc in the sheep red blood cells and S. saprophyticus. Since GlcNAc-BSA contains N-acetylglucosamine to which wheat germ agglutinin can bind, it is most likely that an interaction between a wheat germ agglutinin-bindable substance in S. saprophyticus and an N-acetylglucosamine-bindable substance in sheep red blood cells is involved in the agglutination.