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Updated: Feb 12, 2026
High Yield Purification of Plasmodium falciparum Merozoites For Use in Opsonizing Antibody Assays
Published on: July 17, 2014
The malaria parasite Plasmodium falciparum Sortilin is essential for merozoite formation and apical complex
Stéphanie Hallée1, Natalie A Counihan2, Kathryn Matthews2
1Centre de recherche en infectiologie, CHU de Québec-Université Laval, Quebec City, QC, Canada.
Abstract:
The inner membrane complex and the apical secretory organelles are defining features of apicomplexan parasites. Despite their critical roles, the mechanisms behind the biogenesis of these structures in the malaria parasite Plasmodium falciparum are still poorly defined. We here show that decreasing expression of the P. falciparum homologue of the conserved endolysomal escorter Sortilin-VPS10 prevents the formation of the inner membrane complex and abrogates the generation of new merozoites. Moreover, protein trafficking to the rhoptries, the micronemes, and the dense granules is disrupted, which leads to the accumulation of apical complex proteins in the endoplasmic reticulum and the parasitophorous vacuole. We further show that protein export to the erythrocyte and transport through the constitutive secretory pathway are functional. Taken together, our results suggest that the malaria parasite P. falciparum Sortilin has potentially broader functions than most of its other eukaryotic counterparts.
Insights
Sortilin in Plasmodium falciparum is crucial for forming the inner membrane complex and generating new merozoites. Its disruption impairs protein trafficking to apical organelles, impacting malaria parasite development.
Area of Science:
- Cell biology
- Parasitology
- Molecular biology
Background:
- Apicomplexan parasites, including the malaria parasite Plasmodium falciparum, possess unique structures like the inner membrane complex and apical secretory organelles.
- The biogenesis mechanisms for these critical structures in P. falciparum remain largely unelucidated.
Purpose of the Study:
- To investigate the role of the P. falciparum homologue of Sortilin-VPS10 in the biogenesis of the inner membrane complex and apical organelle formation.
- To understand the impact of Sortilin dysfunction on protein trafficking and parasite development.
Main Methods:
- Gene expression knockdown of the P. falciparum Sortilin homologue.
- Analysis of inner membrane complex formation.
- Assessment of merozoite generation.
- Protein trafficking studies to apical organelles (rhoptries, micronemes, dense granules).
- Localization studies of apical complex proteins.
Main Results:
- Decreased Sortilin expression prevented inner membrane complex formation and merozoite generation.
- Protein trafficking to rhoptries, micronemes, and dense granules was disrupted.
- Apical complex proteins accumulated in the endoplasmic reticulum and parasitophorous vacuole.
- Protein export to the erythrocyte and constitutive secretory pathway transport remained functional.
Conclusions:
- P. falciparum Sortilin plays a vital role in the biogenesis of the inner membrane complex and apical organelle formation.
- Sortilin dysfunction leads to significant defects in protein trafficking essential for parasite development.
- The function of P. falciparum Sortilin appears broader than its counterparts in other eukaryotes.
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