Using the PfEMP1 head structure binding motif to deal a blow at severe malaria

Plasmodium falciparum (Pf) malaria causes 200 million cases worldwide, 8 million being severe and complicated leading to ∼1 million deaths and ∼100,000 abortions annually. Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) has been implicated in cytoadherence and infected erythrocyte rose...

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Veröffentlicht in:PloS one 2014-02, Vol.9 (2), p.e88420-e88420
Hauptverfasser: Patarroyo, Manuel E, Alba, Martha Patricia, Curtidor, Hernando, Vanegas, Magnolia, Almonacid, Hannia, Patarroyo, Manuel A
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Alba, Martha Patricia
Curtidor, Hernando
Vanegas, Magnolia
Almonacid, Hannia
Patarroyo, Manuel A
description Plasmodium falciparum (Pf) malaria causes 200 million cases worldwide, 8 million being severe and complicated leading to ∼1 million deaths and ∼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 ∼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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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 ∼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. 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subjects Animals
Antigens
Aotidae
Binding
Biology
Chemistry
Chondroitin sulfate
Chondroitin Sulfates - metabolism
Conserved sequence
Endothelial cells
Erythrocyte membrane protein 1
Erythrocytes
Erythrocytes - immunology
Erythrocytes - metabolism
Health sciences
Humans
Hydrogen bonds
Immunity
Immunization
Immunoglobulins
Laboratory animals
Malaria
Malaria Vaccines - immunology
Malaria, Falciparum - immunology
Malaria, Falciparum - metabolism
Malaria, Falciparum - prevention & control
Medicine
Membrane proteins
Monkeys
Monkeys & apes
Parasites
Peptides
Plasmodium falciparum
Pregnancy
Protein Binding - immunology
Proteins
Protozoan Proteins - metabolism
Rosette formation
Sulfates
Vector-borne diseases
Veterinarians
title Using the PfEMP1 head structure binding motif to deal a blow at severe malaria
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