The malaria parasite Plasmodium falciparum Sortilin is essential for merozoite formation and apical complex biogenesis

Cell Microbiol. 2018 Aug;20(8):e12844. doi: 10.1111/cmi.12844. Epub 2018 Apr 30.

Abstract

The inner membrane complex and the apical secretory organelles are defining features of apicomplexan parasites. Despite their critical roles, the mechanisms behind the biogenesis of these structures in the malaria parasite Plasmodium falciparum are still poorly defined. We here show that decreasing expression of the P. falciparum homologue of the conserved endolysomal escorter Sortilin-VPS10 prevents the formation of the inner membrane complex and abrogates the generation of new merozoites. Moreover, protein trafficking to the rhoptries, the micronemes, and the dense granules is disrupted, which leads to the accumulation of apical complex proteins in the endoplasmic reticulum and the parasitophorous vacuole. We further show that protein export to the erythrocyte and transport through the constitutive secretory pathway are functional. Taken together, our results suggest that the malaria parasite P. falciparum Sortilin has potentially broader functions than most of its other eukaryotic counterparts.

Keywords: apical organelles; cell division; escorter; inner membrane complex; malaria; protein trafficking.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Vesicular Transport / genetics
  • Adaptor Proteins, Vesicular Transport / metabolism*
  • Gene Knockdown Techniques
  • Merozoites / growth & development*
  • Organelle Biogenesis*
  • Plasmodium falciparum / growth & development*
  • Protein Transport

Substances

  • Adaptor Proteins, Vesicular Transport
  • sortilin