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

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

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

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 (Pf EMP1) 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.

Original languageEnglish (US)
Article numbere88420
JournalPLOS ONE
Volume9
Issue number2
DOIs
StatePublished - Feb 7 2014

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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