Hemoglobin degradation in the malaria parasite Plasmodium falciparum: An ordered process in a unique organelle

D. E. Goldberg, A. F.G. Slater, A. Cerami, G. B. Henderson

Research output: Contribution to journalArticlepeer-review

369 Scopus citations

Abstract

The malaria parasite Plasmodium falciparum uses host erythrocyte hemoglobin as a major nutrient source. We report the purification of P. falciparum digestive vacuoles and characterization of the degradative process therein. Vacuoles were isolated by a combination of differential centrifugation and density gradient separation. The pure vacuoles were capable of degrading hemoglobin to small fragments with a pH optimum of 5-5.5. Proteolysis in the vacuoles appears to be an ordered process, requiring an aspartic protease to clip intact hemoglobin before other proteolytic activities can function efficiently. The vacuoles do not contain other hydrolases commonly found in lysosomes and therefore appear to be unique proteolytic organelles designed specifically to degrade hemoglobin.

Original languageEnglish
Pages (from-to)2931-2935
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number8
DOIs
StatePublished - Jan 1 1990
Externally publishedYes

Keywords

  • aspartic protease
  • hemozoin
  • lysosomes
  • vacuoles

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