Chromatographic and antigenic properties of Echinococcus granulosus hydatid cyst-derived glycolipids.

The neutral and acidic fraction glycolipids of Echinococcus granulosus metacestode tissue compartments were isolated, defined by their chromatographic and antigenic properties, and assessed as to their efficacy as antigens in the serodiagnosis of human hepatic cystic and alveolar echinococcosis, and other helminthiases. Analyses were accomplished by thin-layer chromatography immunostaining and ELISA. The neutral glycolipid fraction's major carbohydrate epitope was the same as or very similar to that of Taenia crassiceps neutral glyco(sphingo)lipids, as represented by the 'neogala'-series core structure. The blood group-active, carbohydrate epitope P1 was expressed by a number of neutral fraction glycolipid component bands. The reverse-phase, thin-layer chromatography-isolated neutral fraction glycolipid component, designated Ag1, was efficient in the serological discrimination of cystic echinococcosis medium to high-titred sera. Ag1 did not specifically discriminate low-titred sera, i.e., other human helminthiases. The detected sialic acid residues of the acidic fraction glycolipids, on enzymatic cleavage, were identified as N-acylneuraminic acid and terminal. The acidic fraction glycolipids exhibited the paradox of only chemically minor components being antigenic towards cystic and alveolar echinococcosis infection sera. The combined acidic fraction glycolipid components Ra and Rx were capable of serological discrimination between cystic echinococcosis, alveolar echinococcosis and other helminthiases.