Role of nonimmune IgG bound to PfEMP1 in placental malaria

Science. 2001 Sep 14;293(5537):2098-100. doi: 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 beta 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Adhesion
  • Chondroitin ABC Lyase / metabolism
  • Chondroitin Sulfates / metabolism
  • Chondroitin Sulfates / pharmacology
  • Cloning, Molecular
  • Erythrocytes / metabolism
  • Erythrocytes / parasitology*
  • Female
  • Humans
  • Hyaluronic Acid / pharmacology
  • Hyaluronoglucosaminidase / metabolism
  • Immunoglobulin G / immunology
  • Immunoglobulin G / metabolism*
  • Malaria, Falciparum / immunology
  • Malaria, Falciparum / parasitology*
  • Placenta / blood supply
  • Placenta / immunology
  • Placenta / parasitology*
  • Placenta Diseases / immunology
  • Placenta Diseases / parasitology
  • Plasmodium falciparum / genetics
  • Plasmodium falciparum / immunology
  • Plasmodium falciparum / metabolism
  • Pregnancy
  • Pregnancy Complications, Parasitic / immunology
  • Pregnancy Complications, Parasitic / parasitology*
  • Protein Structure, Tertiary
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / immunology
  • Protozoan Proteins / metabolism*
  • Receptors, Fc / metabolism*
  • Recombinant Fusion Proteins
  • Staphylococcal Protein A / metabolism
  • Staphylococcal Protein A / pharmacology
  • Trophoblasts / immunology
  • Trophoblasts / parasitology

Substances

  • Immunoglobulin G
  • Protozoan Proteins
  • Receptors, Fc
  • Recombinant Fusion Proteins
  • Staphylococcal Protein A
  • erythrocyte membrane protein 1, Plasmodium falciparum
  • Hyaluronic Acid
  • Chondroitin Sulfates
  • Hyaluronoglucosaminidase
  • Chondroitin ABC Lyase