Disguising itself--insights into Plasmodium falciparum binding and immune evasion from the DBL crystal structure.
Duffy-binding like (DBL) domains are common to two different families of malaria proteins that are involved in parasite invasion of erythrocytes or cytoadhesion of infected erythrocytes. DBL domain crystal structures have recently been solved for two different erythrocyte binding ligands, EBA-175 and the Plasmodium knowlesi alpha Duffy binding protein. These structures reveal different mechanisms for DBL binding and erythrocyte invasion. This review summarizes recent work on DBL domain binding and immune evasion and proposes a new structural model for how these domains adapted to intense antibody surveillance at the infected erythrocyte surface.
Howell
Dasein P-G
DP
Seattle Biomedical Research Institute, WA 98109-5219, USA.
Samudrala
Ram
R
Smith
Joseph D
JD
D000595:Amino Acid Sequence; D000818:Animals; D000940:Antigenic Variation; D000953:Antigens, Protozoan / Q000737:chemistry* / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D004912:Erythrocytes / Q000469:parasitology; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000737:chemistry* / Q000276:immunology* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D013329:Structure-Activity Relationship
D000953:Antigens, Protozoan; D015815:Cell Adhesion Molecules; C066001:Duffy antigen binding protein, Plasmodium; D015800:Protozoan Proteins; D011956:Receptors, Cell Surface; C065668:erythrocyte-binding antigen 175, Plasmodium