The crystal structure of P. knowlesi DBPα 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 rela...

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Bibliographic Details
Published inTrends in biochemical sciences (Amsterdam. Regular ed.) Vol. 31; no. 9; pp. 487 - 491
Main Authors McHenry, Amy M., Adams, John H.
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 01.09.2006
Subjects
Plasmodium knowlesi
Plasmodium vivax
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Summary: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.
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ISSN:0968-0004
1362-4326
DOI:10.1016/j.tibs.2006.07.003