Evidence that the Malaria Parasite Plasmodium falciparum Putative Rhoptry Protein 2 Localizes to the Golgi Apparatus throughout the Erythrocytic Cycle

PLoS One. 2015 Sep 16;10(9):e0138626. doi: 10.1371/journal.pone.0138626. eCollection 2015.

Abstract

Invasion of a red blood cell by Plasmodium falciparum merozoites is an essential step in the malaria lifecycle. Several of the proteins involved in this process are stored in the apical complex of the merozoite, a structure containing secretory organelles that are released at specific times during invasion. The molecular players involved in erythrocyte invasion thus represent potential key targets for both therapeutic and vaccine-based strategies to block parasite development. In our quest to identify and characterize new effectors of invasion, we investigated the P. falciparum homologue of a P. berghei protein putatively localized to the rhoptries, the Putative rhoptry protein 2 (PbPRP2). We show that in P. falciparum, the protein colocalizes extensively with the Golgi apparatus across the asexual erythrocytic cycle. Furthermore, imaging of merozoites caught at different times during invasion show that PfPRP2 is not secreted during the process instead staying associated with the Golgi apparatus. Our evidence therefore suggests that PfPRP2 is a Golgi protein and that it is likely not a direct effector in the process of merozoite invasion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Southern
  • Blotting, Western
  • Erythrocytes / cytology
  • Erythrocytes / metabolism
  • Erythrocytes / parasitology*
  • Golgi Apparatus / genetics
  • Golgi Apparatus / metabolism*
  • Host-Parasite Interactions
  • Humans
  • Life Cycle Stages
  • Malaria, Falciparum / parasitology*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Merozoites / growth & development
  • Merozoites / metabolism*
  • Merozoites / parasitology
  • Plasmodium falciparum / growth & development*
  • Plasmodium falciparum / pathogenicity
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*

Substances

  • Membrane Proteins
  • Protozoan Proteins
  • ROP 2 protein, Toxoplasma gondii
  • rhoptry associated protein, Plasmodium

Grants and funding

Funding for the study was provided to D.R. by the National Science and Engineering Research Council of Canada (http://www.nserc-crsng.gc.ca), grant number 418192, the Canadian Foundation for Innovation (www.innovation.ca), grant number 29837 and the Banting Foundation New Investigator award. D.R. is supported by a Fond de la Recherche du Québec-Santé Junior 1 career award (http://www.frqs.gouv.qc.ca). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.