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MAP-X reveals distinct protein complex dynamics across Plasmodium falciparum blood stages
Samuel Pazicky1, Seth Tjia1, Guilherme B Farias2,3,4
1School of Biological Sciences, Nanyang Technology University, Singapore, Singapore.
Abstract:
The malaria parasite Plasmodium falciparum undergoes a complex intraerythrocytic developmental cycle (IDC) that relies on a dynamic network of protein-protein interactions. These are usually mapped ex vivo, limiting our understanding of their dynamics and composition in natural environments. Here we introduce the meltome-assisted profiling of protein complexes (MAP-X) that maps the complexome through thermal proteome profiling in intact cells. We applied MAP-X across seven timepoints in the P. falciparum IDC. MAP-X predicted more than 20,000 interactions, resolving conserved protein complexes, reproducing previously identified interactions and finding previously unreported associations. We found that malaria protein complexes undergo distinct dynamic alterations, and we predicted their moonlighting subunits that dissociate from their native complex to assume different biological functions. Altogether, our findings provide a resource for uncovering Plasmodium biology and show that MAP-X can characterize protein complexes in intact cells to reveal cellular physiology at a proteome-wide level.
Insights
We developed meltome-assisted profiling of protein complexes (MAP-X) to study malaria parasite protein interactions within intact cells. This method reveals dynamic changes in protein complexes during the Plasmodium falciparum intraerythrocytic developmental cycle (IDC).
Area of Science:
- Molecular Biology
- Parasitology
- Proteomics
Background:
- The malaria parasite Plasmodium falciparum has a complex intraerythrocytic developmental cycle (IDC).
- Understanding protein-protein interactions within the parasite is crucial but challenging due to ex vivo limitations.
- Existing methods often fail to capture the dynamic nature of protein complexes in their natural cellular environment.
Purpose of the Study:
- To introduce and validate a novel method, meltome-assisted profiling of protein complexes (MAP-X), for mapping protein complexes in intact cells.
- To investigate the dynamic alterations of protein complexes during the Plasmodium falciparum IDC.
- To identify potential moonlighting proteins and their functional roles within the parasite.
Main Methods:
- Development of MAP-X, a technique combining thermal proteome profiling with meltome analysis in intact cells.
- Application of MAP-X across seven distinct timepoints of the P. falciparum IDC.
- Bioinformatic analysis to predict protein-protein interactions and identify protein complexes.
Main Results:
- MAP-X successfully mapped over 20,000 protein-protein interactions during the P. falciparum IDC.
- The study identified conserved and novel protein associations, providing a comprehensive view of the parasite's complexome.
- Distinct dynamic changes in protein complex composition and predicted moonlighting subunits were observed throughout the IDC.
Conclusions:
- MAP-X is a powerful tool for characterizing protein complexes in intact cells, offering insights into cellular physiology at a proteome-wide scale.
- The findings provide a valuable resource for understanding Plasmodium biology and identifying potential therapeutic targets.
- The dynamic nature of protein complexes and the role of moonlighting subunits are critical for parasite survival and development.
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