Role of Nonimmune IgG Bound to PfEMP1 in Placental Malaria
- 14 September 2001
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 293 (5537) , 2098-2100
- https://doi.org/10.1126/science.1062891
Abstract
Infections with Plasmodium falciparum during pregnancy lead to the accumulation of parasitized red blood cells (infected erythrocytes, IEs) in the placenta. IEs of P. falciparum isolates that infect the human placenta were found to bind immunoglobulin G (IgG). A strain of P. falciparum cloned for IgG binding adhered massively to placental syncytiotrophoblasts in a pattern similar to that of natural infections. Adherence was inhibited by IgG-binding proteins, but not by glycosaminoglycans or enzymatic digestion of chondroitin sulfate A or hyaluronic acid. Normal, nonimmune IgG that is bound to a duffy binding–like domain β of the P. falciparum erythrocyte membrane protein 1 (PfEMP1) might at the IE surface act as a bridge to neonatal Fc receptors of the placenta.Keywords
This publication has 13 references indexed in Scilit:
- Plasma Antibodies from Malaria-Exposed Pregnant Women Recognize Variant Surface Antigens on Plasmodium falciparum-Infected Erythrocytes in a Parity-Dependent Manner and Block Parasite Adhesion to Chondroitin Sulfate AThe Journal of Immunology, 2000
- Adhesion of Plasmodium falciparum-infected erythrocytes to hyaluronic acid in placental malariaNature Medicine, 2000
- Plasmodium falciparum domain mediating adhesion to chondroitin sulfate A: A receptor for human placental infectionProceedings of the National Academy of Sciences, 1999
- Antigenic variation in malaria: in situ switching, relaxed and mutually exclusive transcription of var genes during intra-erythrocytic development in Plasmodium falciparumThe EMBO Journal, 1998
- Adherence of Plasmodium falciparum to Chondroitin Sulfate A in the Human PlacentaScience, 1996
- Novel fibrillar structure confers adhesive property to malaria–infected erythrocytesNature Medicine, 1996
- Chondroitin-4-sulphate (proteoglycan) a receptor for Plasmodium falciparum-infected erythrocyte adherence on brain microvascular endothelial cellsResearch in Immunology, 1995
- Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes.The Journal of Experimental Medicine, 1995
- Malaria during pregnancy: A priority area of malaria research and controlParasitology Today, 1995
- Development of γG, γA, γM, β1C/β1A, C′1 esterase inhibitor, ceruloplasmin, transferrin, hemopexin, haptoglobin, fibrinogen, plasminogen, α1-antitrypsin, orosomucoid, β-lipoprotein, α2-macroglobulin, and prealbumin in the human conceptusJournal of Clinical Investigation, 1969