Identification of a 67-amino-acid region of the Plasmodium falciparum variant surface antigen that binds chondroitin sulphate A and elicits antibodies reactive with the surface of placental isolates.

摘要: Summary The complications of malaria in pregnancy are caused by the massive sequestration parasitized erythrocytes (PE) placenta. Placental isolates Plasmodium falciparum unusual that they do not bind primary microvasculature receptor CD36 but instead chondroitin sulphate A (CSA). Preg- nant mothers develop antibodies recognize pla- cental variants worldwide, suggesting a vaccine against is possible. Some mem- bers Duffy binding-like g (DBL- ) domain large and diverse P. erythrocyte membrane protein-1 (PfEMP-1) family, when expressed on Chi- nese hamster ovary (CHO) cells, CSA. To char- acterize better molecular requirements for DBL- adhesion to CSA, we determined binding vari- ous domains. Most did no conserved region was identified strictly differentiated binders from non-binders. Structure- function analysis FCR3-CSA localized minimal CSA 67- residue fragment. This partially among some sequences. Serum rabbit immunized with reacted CSA-binding parasite lines, non-CSA- adherent PE lines adhered other receptors. identification highly variable cytoadherent family may have application pregnancy.