The structure of the Plasmodium falciparum EBA175 ligand domain and the molecular basis of host specificity

Trends Parasitol. 2006 Apr;22(4):143-5. doi: 10.1016/j.pt.2006.02.007. Epub 2006 Feb 23.

Abstract

Erythrocyte-binding antigen 175 (EBA175) is one of the best-characterized Plasmodium falciparum merozoite ligands; the recently solved crystal structure of EBA175 reveals that terminal sialic acids on the erythrocyte glycoprotein glycophorin A are a crucial factor for erythrocyte recognition by EBA175 because they lock into pockets on its surface. Comparison with Plasmodium reichenowi EBA175 indicates that these interactions have a pivotal role in the host-specific adaptations of parasite ligands.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, Protozoan / chemistry*
  • Antigens, Protozoan / physiology*
  • Biological Evolution
  • Erythrocytes / metabolism
  • Erythrocytes / parasitology*
  • Glycophorins / metabolism
  • Host-Parasite Interactions
  • Humans
  • Ligands
  • Plasmodium falciparum / chemistry*
  • Plasmodium falciparum / pathogenicity*
  • Plasmodium falciparum / physiology
  • Polysaccharides / metabolism
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / physiology*

Substances

  • Antigens, Protozoan
  • Glycophorins
  • Ligands
  • Polysaccharides
  • Protozoan Proteins
  • erythrocyte-binding antigen 175, Plasmodium