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Methods to Investigate the Regulatory Role of Small RNAs and Ribosomal Occupancy of Plasmodium falciparum
Published on: December 4, 2015
Time-resolved proximity biotinylation implicates a porin protein in export of transmembrane malaria parasite
David Anaguano1,2, Watcharatip Dedkhad1,2, Carrie F Brooks2
1Department of Cellular Biology, University of Georgia, Athens, GA, USA.
Abstract:
The malaria-causing parasite, Plasmodium falciparum completely remodels its host red blood cell (RBC) through the export of several hundred parasite proteins, including transmembrane proteins, across multiple membranes to the RBC. However, the process by which these exported membrane proteins are extracted from the parasite plasma membrane for export remains unknown. To address this question, we fused the exported membrane protein, skeleton binding protein 1 (SBP1), with TurboID, a rapid, efficient and promiscuous biotin ligase (SBP1TbID). Using time-resolved proximity biotinylation and label-free quantitative proteomics, we identified two groups of SBP1TbID interactors - early interactors (pre-export) and late interactors (post-export). Notably, two promising membrane-associated proteins were identified as pre-export interactors, one of which possesses a predicted translocon domain, that could facilitate the export of membrane proteins. Further investigation using conditional mutants of these candidate proteins showed that these proteins were essential for asexual growth and localize to the host-parasite interface during early stages of the intraerythrocytic cycle. These data suggest that they might play a role in ushering membrane proteins from the parasite plasma membrane for export to the host RBC.
Insights
Researchers identified key proteins involved in exporting malaria parasite membrane proteins to host red blood cells. These proteins are crucial for parasite growth and function during infection.
Area of Science:
- Malariology
- Cell Biology
- Parasitology
Background:
- Plasmodium falciparum remodels host red blood cells (RBCs) by exporting hundreds of parasite proteins.
- The mechanism for exporting transmembrane proteins from the parasite plasma membrane is unknown.
Purpose of the Study:
- To investigate the process of extracting exported membrane proteins from the parasite plasma membrane for export.
- To identify host-parasite interface proteins involved in membrane protein export.
Main Methods:
- Used a fusion protein (SBP1TbID) combining skeleton binding protein 1 (SBP1) with TurboID.
- Employed time-resolved proximity biotinylation and label-free quantitative proteomics.
- Generated conditional mutants of candidate export proteins.
Main Results:
- Identified early (pre-export) and late (post-export) interactors of SBP1TbID.
- Discovered two membrane-associated proteins as pre-export interactors, one with a putative translocon domain.
- Demonstrated these candidate proteins are essential for asexual growth and localize to the host-parasite interface.
Conclusions:
- The identified proteins may facilitate the export of membrane proteins from the parasite plasma membrane.
- These proteins likely play a role in ushering membrane proteins for export to the host RBC.
- This study sheds light on a critical step in malaria parasite invasion and host cell manipulation.
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