Related Experiment Video
Updated: Feb 19, 2026
CRISPR/Cas9 Gene Editing to Make Conditional Mutants of Human Malaria Parasite P. falciparum
Published on: September 18, 2018
Plasmodium falciparum exported protein PFE60 influences Maurer's clefts architecture and virulence complex
Meng Zhang1, Pierre Faou2, Alexander G Maier1
1Research School of Biology, The Australian National University, Canberra, ACT 2601, Australia.
Abstract:
Plasmodium falciparum, the most lethal malaria parasite species for humans, vastly remodels the mature erythrocyte host cell upon invasion for its own survival. Maurer's clefts (MC) are membraneous structures established by the parasite in the cytoplasm of infected cells. These organelles are deemed essential for trafficking of virulence complex proteins. The display of the major virulence protein, P. falciparum erythrocyte membrane protein 1 (PfEMP1) on the surface of the infected red blood cell and the subsequent cytoadhesion of infected cells in the microvasculature of vital organs is the key mechanism that leads to the pathology associated with malaria infection. In a previous study we established that PFE60 (PIESP2) is one of the protein components of this complex. Here we demonstrate that PFE60 plays a role in MC lamella segmentation since in the absence of the protein, infected cells display a higher number of stacked MC compared with wild type infected red blood cells. Also, another exported parasite protein (Pf332) failed to localise correctly to the MC in cells lacking PFE60. Furthermore - unlike all other described resident MC membrane proteins - PFE60 does not require its transmembrane regions to be targeted to the organelle. We also provide further evidence that PFE60 is not a red blood cell surface antigen.
Insights
The malaria parasite Plasmodium falciparum remodels host cells using Maurer's clefts (MC). The protein PFE60 is crucial for MC structure and function, impacting virulence protein transport and malaria pathology.
Area of Science:
- Cell biology
- Parasitology
- Molecular biology
Background:
- Plasmodium falciparum causes severe malaria by altering infected erythrocytes.
- Maurer's clefts (MC) are key parasite-derived organelles essential for virulence factor transport.
- PfEMP1 display on infected red blood cells mediates cytoadhesion and pathology.
Purpose of the Study:
- To investigate the role of PFE60 (PIESP2) in the biogenesis and function of Maurer's clefts.
- To determine the localization mechanism of PFE60 within the infected erythrocyte.
- To assess the impact of PFE60 absence on MC structure and protein trafficking.
Main Methods:
- Genetic manipulation of P. falciparum to generate PFE60-deficient parasites.
- Microscopy techniques to analyze MC morphology and protein localization.
- Biochemical assays to investigate protein targeting mechanisms.
Main Results:
- PFE60 is essential for MC lamella segmentation, with its absence leading to stacked MC structures.
- The exported protein Pf332 fails to localize correctly to MC in PFE60-deficient cells.
- PFE60 targets MC independently of its transmembrane domains, unlike other MC proteins.
Conclusions:
- PFE60 plays a critical role in the structural organization and protein trafficking functions of Maurer's clefts.
- PFE60's unique targeting mechanism highlights novel aspects of organelle biogenesis in infected erythrocytes.
- Understanding PFE60's function offers insights into malaria pathogenesis and potential therapeutic targets.
Related Concept Videos
01:27Diversity of Protists II
00:58Symbiosis
01:28Fungal Phylum Microsporidia