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J Infect Dis. 2007 Aug 15;196(4):617-21. Epub 2007 Jun 29.

Members of the low-molecular-mass rhoptry protein complex of Plasmodium falciparum bind to the surface of normal erythrocytes.

Author information

1
Unite de Biologie des Interactions Hote-Parasite Centre National de la Recherche Scientifique-Unite de Recherche Associee 2581, Institut Pasteur, Paris, France.

Abstract

The destruction of erythrocytes is one of the most frequently observed causes of severe malarial anemia. Recently, we showed that tagging normal erythrocytes and cells of erythroid precursors with rhoptry-derived proteins can trigger their destruction. In the present study, we used rhoptry-associated protein (RAP)-1 and RAP-3 gene-disruption mutant Plasmodium falciparum parasites and showed that 2 members of a rhoptry protein complex, RAP-1 and RAP-2, bind to the surface of normal erythrocytes. Surface iodination experiments showed that RAP-1 but not RAP-3 mutant parasites lose their capacity to tag erythrocytes. This work opens new doors into the investigation of the molecular mechanism of anemia in patients with malaria.

PMID:
17624849
DOI:
10.1086/519685
[Indexed for MEDLINE]

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