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© Artur Scherf
Scanning Electron Microscopy of Red Blood Cell infected by Plasmodium falciparum.
Publication : The Journal of infectious diseases

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of infectious diseases - 29 Jun 2007

Sterkers Y, Scheidig C, da Rocha M, Lepolard C, Gysin J, Scherf A

Link to Pubmed [PMID] – 17624849

J. Infect. Dis. 2007 Aug;196(4):617-21

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.

http://www.ncbi.nlm.nih.gov/pubmed/17624849