0000000000867224
AUTHOR
S. G. Gatermann
The hemagglutinin of Staphylococcus saprophyticus is a major adhesin for uroepithelial cells.
The 160-kDa hemagglutinin of Staphylococcus saprophyticus also serves as a fibronectin-binding protein, and the two activities may be present on different parts of the molecule. Bacteria expressing the 160-kDa hemagglutinin bound in large numbers to histological sections of human ureters, whereas nonhemagglutinating bacteria did not bind. Binding was decreased by an antiserum to the 160-kDa protein and by a preparation of sheep erythrocyte membranes. Fibronectin had no effect. We therefore conclude that binding of S. saprophyticus to uroepithelial cells is mediated by the hemagglutinating activity of the 160-kDa surface protein.
The hemagglutinin of Staphylococcus saprophyticus binds to a protein receptor on sheep erythrocytes.
Staphylococcus saprophyticus, an important cause of urinary tract infections, produces two major surface proteins, the S. saprophyticus surface-associated protein (Ssp) and the hemagglutinin, which mediates fibronectin binding and also functions as the major adhesion of the organism. The hemagglutinating and fibronectin binding functions probably reside on different parts of the molecule. To identify a receptor on eukaryotic cells, binding and inhibition studies with acidic and neutral glycosphingolipids, carbohydrates, and proteins of sheep erythrocyte membranes were conducted. S. saprophyticus did not bind to any glycosphingolipid and no inhibition was observed when hemagglutination assay…