The binding of human low-density lipoproteins to the surface of schistosomula of Schistosoma mansoni is inhibited by polyanions and reduces the binding of anti-schistosomal antibodies.
Host molecules such as serum lipoproteins, blood group glycolipids, and histocompatibility antigens may bind to schistosomes and thereby prevent immune recognition of the parasite. This study examines the kinetics of lipoprotein binding, the ability of polyanions to inhibit lipoprotein binding, the binding of anti-schistosomal antibodies to worms that have previously bound low-density lipoprotein (LDL), and the distribution of lipoproteins bound to the parasites. Lipoproteins in human serum (HS) and purified LDL, very low-density lipoprotein (VLDL), and apolipoprotein B (apo B) in defined media were demonstrated on the surface of schistosomula of Schistosoma mansoni by fluorescence and immunoelectron microscopy using a polyclonal goat anti-human apolipoprotein B antibody (anti-apo B). By fluorophotometric microscopy, lipoprotein binding began within 15 minutes and was largely completed within 3 hours of exposure. Lipoprotein binding saturated at 10% HS or 20 micrograms protein/300 microliters of purified LDL. Suramin inhibited LDL binding by 59% in a dose-dependent fashion. In the absence of LDL in the medium, 2 mM suramin dissociated 41% of bound LDL from the worm surface within 15 minutes and 10 mg/ml heparin dissociated 36%. The binding of human anti-schistosomal antibodies to schistosomula was inhibited by bound LDL. By fluorescence microscopy, serum or purified lipoproteins were distributed over the entire surface of the parasite with focal areas of high intensity. Ultrastructurally, reaction product was seen on the outer leaflet of the outer tegumental membrane and in aggregates and surrounding vesicular structures varying in diameter from 13 to 83 nm. These studies demonstrate that lipoproteins bind to the surface of schistosomula. The binding of lipoproteins is partially inhibited by polyanions, reduces the binding of human anti-schistosomal antibodies, and may help the parasite escape the immune response.
Chiang
C P
CP
Department of Rheumatology/Immunology, Harvard Medical School, Boston, Massachusetts.
Caulfield
J P
JP
D000818:Animals; D000909:Antibodies, Helminth / Q000378:metabolism*; D001055:Apolipoproteins B / Q000378:metabolism; D001667:Binding, Competitive / Q000187:drug effects; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D006493:Heparin / Q000494:pharmacology; D006801:Humans; D008077:Lipoproteins, LDL / Q000378:metabolism*; D008079:Lipoproteins, VLDL / Q000378:metabolism; D011485:Protein Binding; D012550:Schistosoma mansoni / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D013498:Suramin / Q000494:pharmacology
D000909:Antibodies, Helminth; D001055:Apolipoproteins B; D008077:Lipoproteins, LDL; D008079:Lipoproteins, VLDL; D013498:Suramin; D006493:Heparin