Characterization of the hemagglutinin of Staphylococcus epidermidis.

Adherence to biomaterials and production of biofilm is thought to be pivotal in the pathogenesis of prosthetic device infection by Staphylococcus epidermidis. In this study a strong association (P < .001) of hemagglutination with adherence and biofilm production was observed. Hemagglutination was not associated with cell surface hydrophobicity (P = .906). Hemagglutination inhibition studies revealed that hemagglutination was not affected by heat, pH, cation concentration, proteolytic enzymes, biologic detergent, serum proteins, or subinhibitory antibiotics. Hemagglutination was abolished by periodate oxidation and digestion with glycosidases. It was markedly inhibited by beta-lactose and its monosaccharide constituents in a concentration-dependent fashion. Hemagglutinin expression depended on the presence of glucose. Chemical analysis of a partially purified hemagglutinin preparation and cell-free hemagglutinating supernatants revealed little or no protein and small quantities of reducing sugars, pentose, ketose, hexosamine, uronic acid, and phosphate. Hemagglutinin of S. epidermidis appears to be a polysaccharide distinct from other known adhesins of S. epidermidis.