The structure of the Plasmodium falciparum EBA175 ligand domain and the molecular basis of host specificity.
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.
Division of Geographic Medicine, University of Alabama at Birmingham, Birmingham, AL 35294-2170, USA.
Debasish
D
Chattopadhyay
Julian
J
Rayner
Amy M
AM
McHenry
John H
JH
Adams
D000818:Animals; D000953:Antigens, Protozoan / Q000737:chemistry* / Q000502:physiology*; D005075:Biological Evolution; D004912:Erythrocytes / Q000378:metabolism / Q000469:parasitology*; D006021:Glycophorins / Q000378:metabolism; D006790:Host-Parasite Interactions; D006801:Humans; D008024:Ligands; D010963:Plasmodium falciparum / Q000737:chemistry* / Q000472:pathogenicity* / Q000502:physiology; D011134:Polysaccharides / Q000378:metabolism; D015800:Protozoan Proteins / Q000737:chemistry* / Q000502:physiology*
D000953:Antigens, Protozoan; D006021:Glycophorins; D008024:Ligands; D011134:Polysaccharides; D015800:Protozoan Proteins; C065668:erythrocyte-binding antigen 175, Plasmodium