Demonstration of soluble Plasmodium falciparum antigens reactive with Limulus amoebocyte lysate and polymyxin B.

To investigate whether soluble Plasmodium falciparum antigens possess endotoxin-like properties, the interaction of Limulus amoebocyte lysate (LAL) with defined soluble antigens from Plasmodium falciparum was studied by various crossed immunoelectrophoretic methods and immunoblotting. The soluble P. falciparum antigens were purified by affinity chromatography using human IgG from malaria-immune adults as ligand. Of eight possible antigens, at least three were affected by LAL, as indicated by disappearance of these antigens in the precipitation pattern, after the reaction with LAL. One of the LAL-reactive antigens is a heat-stable glycoprotein with the presence of both hydrophilic and hydrophobic regions in its structure. This antigen shows a strong reaction with polymyxin B, and antibodies against it have been shown to be inhibitory to the growth of P. falciparum in culture. It is concluded that LAL reacts with several soluble antigens from P. falciparum and it is suggested that these antigens participate in the induction of protective immunity to malaria, and consequently that one or more of the soluble antigens are candidates for a malaria vaccine.