Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum

Michael Klemba, Wandy Beatty, Ilya Gluzman, Daniel E. Goldberg

Research output: Contribution to journalArticlepeer-review

107 Scopus citations

Abstract

A family of aspartic proteases, the plasmepsins (PMs), plays a key role in the degradation of hemoglobin in the Plasmodium falciparum food vacuole. To study the trafficking of proPM II, we have modified the chromosomal PM II gene in P falciparum to encode a proPM II-GFP chimera. By taking advantage of green fluorescent protein fluorescence in live parasites, the ultrastructural resolution of immunoelectron microscopy, and inhibitors of trafficking and PM maturation, we have investigated the biosynthetic path leading to mature PM II in the food vacuole. Our data support a model whereby proPM II is transported through the secretory system to cytostomal vacuoles and then is carried along with its substrate hemoglobin to the food vacuole where it is proteolytically processed to mature PM II.

Original languageEnglish
Pages (from-to)47-56
Number of pages10
JournalJournal of Cell Biology
Volume164
Issue number1
DOIs
StatePublished - Jan 2004

Keywords

  • Brefeldin A
  • Endoplasmic reticulum
  • Hemoglobin
  • Protease
  • Protein trafficking

Fingerprint

Dive into the research topics of 'Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum'. Together they form a unique fingerprint.

Cite this