Schistosoma mansoni:l-lysil residues in agglutination of mouse erythrocytes by acid phospholipids of parasite membranes

Abstract

The agglutination of mouse erythrocytes caused by acid phospholipids of Schistosoma mansoni membranes is strongly inhibited by l-lysine; other amino acids do not interfere with the reaction. The inhibitory effect observed after treatment of mouse erythrocytes with low concentrations of glutaraldehyde confirms that l-lysil residues are present on the surface of the erythrocytes and that, probably, protonated ϵ-amino groups are responsible for the susceptibility of these cells to the agglutination by worm membranes in physiological conditions. There is a possible role for lysil-phospholipid interactions in the host-parasite relationships.