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<p>The malaria parasite <i>Plasmodium falciparum</i> 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 <i>P. falciparum</i> 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 <i>Plasmodium</i> biology and show that MAP-X can characterize protein complexes in intact cells to reveal cellular physiology at a proteome-wide level.</p>

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MAP-X reveals distinct protein complex dynamics across Plasmodium falciparum blood stages

  • 期刊论文

  • 发表日期：

    2025年11月28日

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  • Samuel Pazicky,
  • Seth Tjia,
  • Guilherme B. Farias,
  • Nick Piwon,
  • Nisha Philip,
  • Radoslaw M. Sobota,
  • Andrew P. Waters,
  • Tim-Wolf Gilberger,
  • Zbynek Bozdech

摘要

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.