Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum

Science. 1994 Jun 24;264(5167):1941-4. doi: 10.1126/science.8009226.

Abstract

A 175-kilodalton erythrocyte binding protein, EBA-175, of the parasite Plasmodium falciparum mediates the invasion of erythrocytes. The erythrocyte receptor for EBA-175 is dependent on sialic acid. The domain of EBA-175 that binds erythrocytes was identified as region II with the use of truncated portions of EBA-175 expressed on COS cells. Region II, which contains a cysteine-rich motif, and native EBA-175 bind specifically to glycophorin A, but not to glycophorin B, on the erythrocyte membrane. Erythrocyte recognition of EBA-175 requires both sialic acid and the peptide backbone of glycophorin A. The identification of both the receptor and ligand domains may suggest rational designs for receptor blockade and vaccines.

MeSH terms

  • Animals
  • Antigens, Protozoan*
  • Base Sequence
  • Binding Sites
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Line
  • Erythrocytes / metabolism
  • Erythrocytes / parasitology*
  • Glycopeptides / chemistry
  • Glycopeptides / metabolism
  • Glycophorins / chemistry
  • Glycophorins / metabolism*
  • Molecular Sequence Data
  • Plasmodium falciparum / metabolism*
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Sialic Acids / metabolism*

Substances

  • Antigens, Protozoan
  • Carrier Proteins
  • Glycopeptides
  • Glycophorins
  • Protozoan Proteins
  • Recombinant Fusion Proteins
  • Sialic Acids
  • erythrocyte-binding antigen 175, Plasmodium