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Author Spotlight: Identifying Compensatory Pathways in Malaria Parasites Containing Hypomorphic Allele of Essential Protein Kinases
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Author Spotlight: Identifying Compensatory Pathways in Malaria Parasites Containing Hypomorphic Allele of Essential Protein Kinases

Published on: November 22, 2024

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An essential adaptor for apicoplast fission and inheritance in malaria parasites

James A Blauwkamp1,2, Krithika Rajaram2,3, Sophia R Staggers4

  • 1Indiana University School of Medicine, Department of Biochemistry, Molecular Biology and Pharmacology, Indianapolis, USA.

Nature Communications
|November 27, 2025
PubMed

Insights

A newly discovered protein, PfAnchor, is essential for apicoplast fission in malaria parasites. Its disruption halts organelle division, proving crucial for parasite survival and a potential antimalarial drug target.

Area of Science:

  • Malariology
  • Cell Biology
  • Parasitology

Background:

  • The apicoplast, a vital organelle in Plasmodium falciparum, is essential for parasite survival.
  • Apicoplast inheritance during parasite division requires precise positioning and fission, but the underlying mechanisms are unclear.
  • Targeting the apicoplast offers a promising strategy for antimalarial drug development.

Purpose of the Study:

  • To identify key regulators of apicoplast fission and inheritance in Plasmodium falciparum.
  • To elucidate the molecular mechanisms governing apicoplast division in asexual blood-stage parasites.
  • To explore the apicoplast's unique division process as a potential therapeutic vulnerability.

Main Methods:

  • Ultrastructure Expansion Microscopy (U-ExM) to visualize PfAnchor localization.
  • Conditional depletion of PfAnchor to assess its function.
  • Immunoprecipitation to identify interacting proteins, including PfDyn2.
  • Azithromycin treatment to investigate rescue effects on apicoplast structure.

Main Results:

  • PfAnchor localizes to the apicoplast throughout the asexual blood-stage.
  • Conditional depletion of PfAnchor inhibits apicoplast fission, leading to incomplete cytokinesis and parasite death.
  • PfAnchor interacts with PfDyn2, a dynamin-like GTPase involved in organelle fission.
  • Azithromycin-induced disruption of apicoplast structure rescues fission defects caused by PfAnchor depletion.

Conclusions:

  • PfAnchor is an essential regulator of apicoplast fission and inheritance in Plasmodium falciparum.
  • PfAnchor acts as the first identified apicoplast-specific dynamin adaptor protein.
  • Targeting parasite-specific organelle division mechanisms, like those involving PfAnchor, presents a novel antimalarial intervention strategy.

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