Ganglioside modulation of lipopolysaccharide-initiated complement activation. 
Highly purified preparations of mouse gangliosides have been demonstrated to bind to purified preparations of lipopolysaccharide (LPS).  In some instances, the binding has been demonstrated to be dependent upon the presence of sialic acid in the ganglioside preparation.  The binding of gangliosides to LPS from the deep rough Salmonella minnesota Re mutant has suggested that the interaction involves the lipid A-2-keto-3-deoxyoctulosanate region of the LPS macromolecule.  The interaction between gangliosides and LPS has been demonstrated to result in an abrogation of lipid A dependent activation of the classical pathway of serum complement by Re LPS.  Surprisingly, however, the presence of sialic acid containing glycolipids has been shown to enhance significantly the capacity of LPS to initiate activation of the alternative pathway of complement.  These data suggest that sialic acid can enhance as well as inhibit the formation of a stable alternative-pathway C3 convertase.