The crystal structure of P. knowlesi DBPalpha DBL domain and its implications for immune evasion.
Plasmodium vivax invasion of human erythrocytes requires that the ligand domain of the Duffy-binding protein (DBP) recognize its cognate erythrocyte receptor, making DBP a potential target for therapy. The recently determined crystal structure of the orthologous DBP ligand domain of the closely related simian malaria parasite Plasmodium knowlesi provides insight into the molecular basis for receptor recognition and raises important questions about the mechanism of immune evasion employed by the malaria parasite.
McHenry
Amy M
AM
Department of Biological Sciences, PO Box 369, University of Notre Dame, Notre Dame, IN 46556-0369, USA.
Adams
John H
JH
D000818:Animals; D000953:Antigens, Protozoan / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D016790:Plasmodium knowlesi / Q000737:chemistry* / Q000378:metabolism / Q000472:pathogenicity; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry*; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism
D000953:Antigens, Protozoan; C066001:Duffy antigen binding protein, Plasmodium; D008024:Ligands; D015800:Protozoan Proteins; D011956:Receptors, Cell Surface