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The Plasmodium falciparum Vps4 homolog mediates multivesicular body formation

Mei Yang1, Isabelle Coppens, Steve Wormsley

  • 1Yale University School of Medicine, Department of Medicine, Section of Infectious Disease, 333 Cedar Street, PO Box 208022, New Haven, CT 06520-8022, USA.

Journal of Cell Science
|July 15, 2004
PubMed

Insights

This study investigated endosomal multivesicular bodies in Apicomplexa parasites. Researchers found that Vps4 protein is conserved and essential for forming these structures in Plasmodium falciparum and Toxoplasma gondii.

Area of Science:

  • Cell Biology
  • Parasitology
  • Molecular Biology

Background:

  • Apicomplexan parasites possess unique secretory organelles called rhoptries, crucial for host cell invasion.
  • Rhoptries' internal membranes suggest a resemblance to multivesicular bodies (MVBs).
  • The role of MVB endosomal intermediates in Apicomplexa remains largely unexplored.

Purpose of the Study:

  • To investigate the formation of endosomal multivesicular bodies (MVBs) in Apicomplexa.
  • To determine if the Vps4 protein, a key regulator of MVB formation, is conserved and functional in these parasites.
  • To explore the localization and function of Plasmodium falciparum Vps4 (PfVps4) in host cells and parasites.

Main Methods:

  • Utilized the Plasmodium falciparum Vps4 homolog (PfVps4) as a molecular probe.
  • Examined the localization of endogenous and transgenic PfVps4 in P. falciparum and Toxoplasma gondii.
  • Created and analyzed mutated PfVps4 constructs (blocking ATP hydrolysis or binding) in P. falciparum, T. gondii, and COS cells.
  • Assessed cholesterol enrichment and co-localization with early endosome markers in mutant-induced structures.

Main Results:

  • Endogenous PfVps4 localized to the cytoplasm in P. falciparum trophozoites.
  • Transgenic PfVps4 localized to the cytosol across P. falciparum, T. gondii, and COS cells.
  • Mutant PfVps4 (impaired ATP hydrolysis) localized to large vesicular structures in P. falciparum.
  • Mutant PfVps4 (impaired ATP binding or hydrolysis) induced cholesterol-enriched MVBs in T. gondii and COS cells.
  • Mutant PfVps4 structures in T. gondii co-localized with early endosome markers.

Conclusions:

  • Vps4 function is conserved across diverse phylogenetic groups, including Apicomplexa.
  • Endosomal multivesicular body formation occurs in both Plasmodium falciparum and Toxoplasma gondii.
  • These findings provide insights into the conserved mechanisms of endosomal trafficking in parasites.

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