The adhesion of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A is mediated by P. falciparum erythrocyte membrane protein 1

Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):5198-202. doi: 10.1073/pnas.96.9.5198.

Abstract

Chondroitin sulfate A (CSA) is an important receptor for the sequestration of Plasmodium falciparum in the placenta, but the parasite ligand involved in adhesion has not previously been identified. Here we report the identification of a var gene transcribed in association with binding to CSA and present evidence that the P. falciparum erythrocyte membrane protein 1 product of the gene is the parasite ligand mediating CSA binding. Description of this gene and the implication of P. falciparum erythrocyte membrane protein 1 as the parasite ligand paves the way to a more detailed understanding of the pathogenesis of placental infection and potential therapeutic strategies targeting the interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CHO Cells
  • Cell Adhesion
  • Chondroitin Sulfates / metabolism*
  • Cricetinae
  • Erythrocyte Membrane / metabolism
  • Erythrocytes / metabolism
  • Erythrocytes / parasitology*
  • Erythrocytes / pathology
  • Female
  • Humans
  • Ligands
  • Malaria, Falciparum / parasitology*
  • Malaria, Falciparum / transmission
  • Molecular Sequence Data
  • Placenta / parasitology
  • Plasmodium falciparum / parasitology
  • Plasmodium falciparum / physiology*
  • Pregnancy
  • Protozoan Proteins / metabolism*

Substances

  • Ligands
  • Protozoan Proteins
  • erythrocyte membrane protein 1, Plasmodium falciparum
  • Chondroitin Sulfates

Associated data

  • GENBANK/AF134154