gms | German Medical Science

12th Malaria Meeting

Malaria Group / Section Antiparasitic Chemotherapy of the Paul-Ehrlich-Society (PEG e. V.) in cooperation with the German Society for Tropical Medicine and International Health (DTG e. V.) and the German Society for Parasitology (DGP e. V.)

14.11. - 15.11.2014, Bonn

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Multimeric protein complexes of Plasmodium falciparum gametocytes associate with a WD40 protein and reassemble following parasite transmission to the mosquito

Meeting Abstract

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  • Andreas von Bohl - Cellular and Applied Infection Biology, RWTH Aachen University, Aachen, Germany
  • Andrea Kuehn - Research Center for Infectious Diseases, University of Wuerzburg, Wuerzburg, Germany
  • Nina Simon - Research Center for Infectious Diseases, University of Wuerzburg, Wuerzburg, Germany
  • Vanesa Nkwouano Ngongang - Research Center for Infectious Diseases, University of Wuerzburg, Wuerzburg, Germany
  • Stefan Baumeister - Parasitology Section, Faculty of Biology, Philipps University Marburg, Marburg, Germany
  • Jude Przyborski - Parasitology Section, Faculty of Biology, Philipps University Marburg, Marburg, Germany
  • Kim C. Williamson - Department of Biology, Loyola University Chicago, Chicago, USA
  • Rainer Fischer - Fraunhofer Institute for Molecular Biology and Applied Ecology, Aachen, Germany
  • Gabriele Pradel - Cellular and Applied Infection Biology, RWTH Aachen University, Aachen, Germany; Research Center for Infectious Diseases, University of Wuerzburg, Wuerzburg, Germany

12th Malaria Meeting. Bonn, 14.-15.11.2014. Düsseldorf: German Medical Science GMS Publishing House; 2014. Doc14mal01

doi: 10.3205/14mal01, urn:nbn:de:0183-14mal016

Veröffentlicht: 17. Dezember 2014

© 2014 von Bohl et al.
Dieser Artikel ist ein Open Access-Artikel und steht unter den Creative Commons Lizenzbedingungen (http://creativecommons.org/licenses/by-nc-nd/3.0/deed.de). Er darf vervielfältigt, verbreitet und öffentlich zugänglich gemacht werden, vorausgesetzt dass Autor und Quelle genannt werden.

Gliederung

Text

During differentiation in the human host, the gametocytes of Plasmodium falciparum display a remarkable number of adhesive proteins on their plasma membrane. These include the PfCCp protein family, six secreted proteins that assemble to multimeric protein complexes (MPCs) within the parasitophorous vacuole. We previously showed that the MPCs are linked to the gametocyte surface via the protein interaction of PfCCp4 with Pfs230, a binding partner of the GPI-anchored Pfs48/45. We now show that lack of Pfs230 in Pfs230-deficient gametocytes results in the destabilization of the parasitophorous vacuolar space. Pfs230 is known to be cleaved at its N-terminal end, once the gametocytes are taken up by blood-feeding mosquitoes and gametogenesis is initiated in the mosquito midgut. Via co-immunoprecipitation assays followed by Western blotting, we demonstrate that Pfs230 processing results in its increased interaction with the MPC, and that impaired Pfs230 processing causes the release of selected PfCCp proteins from the MPC into the medium. We further identified a new MPC interaction partner via co-immunoprecipitation followed by mass spectrometry, the WD40 domain-repeat protein-like protein PfWLP1. WD40 domains are highly conserved among eukaryotes and known to function in MPC assembly by serving as a rigid scaffold for protein interactions. We show that PfWLP1 is expressed both in asexual blood stage parasites and gametocytes. In gametocytes PfWLP1 is primarily associated with the gametocyte surface and here interacts with MPC components. Reverse genetics failed to disrupt the pfwlp1 gene, while hemagglutinin tagging was feasible, suggesting a crucial function for PfWLP1 during blood stage replication. This is the first report on a plasmodial WD40 protein in MPC assembly.

Note: The authors Andreas von Bohl, Andrea Kuehn, and Nina Simon contributed equally.