Characterization of purified hemagglutinin from non-fimbriated Prevotella intermedia

Abstract

Previous study have shown that partially purified hemagglutinin isolated from non-fimbriated Prevotella intermedia strain E18 can be further purified by arginine agarose and gel filtration. We characterized a purified hemagglutinin from this strain. Hemagglutination activity was sensitive to heat and proteolytic enzymes such as trypsin, chymotrypsin and protease. Addition of D-glucosamine, D-galactosamine, N-acetylneuraminic acid, L-lysine and L-arginine caused hemagglutination inhibition, suggesting that a common component in the above sugars and amino acid may be associated with receptors for hemagglutinin. Hemagglutination activity of the hemagglutinin was eliminated by anti-hemagglutinin serum. These results indicate that non-fimbriated hemagglutinin in this study is quite similar to a hemagglutinin derived from Prevotella intermedia fimbriae.