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Using the PfEMP1 Head Structure Binding Motif to Deal a Blow at Severe Malaria

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Patarroyo, Manuel E.
Patricia Alba, Martha
Curtidor, Hernando
Vanegas, Magnolia
Almonacid, Hannia
Patarroyo, Manuel A.

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2014-02

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Universidad del Rosario

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Abstract
Plasmodium falciparum (Pf) malaria causes 200 million cases worldwide, 8 million being severe and complicated leading to similar to 1 million deaths and similar to 100,000 abortions annually. Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) has been implicated in cytoadherence and infected erythrocyte rosette formation, associated with cerebral malaria; chondroitin sulphate-A attachment and infected erythrocyte sequestration related to pregnancy-associated malaria and other severe forms of disease. An endothelial cell high activity binding peptide is described in several of this similar to 300 kDa hypervariable protein's domains displaying a conserved motif (GACxPxRRxxLC); it established H-bonds with other binding peptides to mediate red blood cell group A and chondroitin sulphate attachment. This motif (when properly modified) induced PfEMP1-specific strain-transcending, fully-protective immunity for the first time in experimental challenge in Aotus monkeys, opening the way forward for a long sought-after vaccine against severe malaria.
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Erythrocyte-membrane PROTEIN-1 , Chondroitin-sulfate-a , Plasmodium-falciparum , Antimalarial Vaccine , Placental Malaria , ALPHA-Domains , Expression , Antibodies , Parasites , Paptides
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