A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites

Catherine Suarez, Gaëlle Lentini, Raghavendran Ramaswamy, Marjorie Maynadier, Eleonora Aquilini, Laurence Berry-Sterkers, Michael Cipriano, Allan L. Chen, Peter Bradley, Boris Striepen, Martin J. Boulanger and Maryse Lebrun ()
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Catherine Suarez: Université de Montpellier
Gaëlle Lentini: Université de Montpellier
Raghavendran Ramaswamy: University of Victoria
Marjorie Maynadier: Université de Montpellier
Eleonora Aquilini: Université de Montpellier
Laurence Berry-Sterkers: Université de Montpellier
Michael Cipriano: University of Pennsylvania
Allan L. Chen: University of California, Los Angeles
Peter Bradley: University of California, Los Angeles
Boris Striepen: University of Pennsylvania
Martin J. Boulanger: University of Victoria
Maryse Lebrun: Université de Montpellier

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract Members of the Apicomplexa phylum, including Plasmodium and Toxoplasma, have two types of secretory organelles (micronemes and rhoptries) whose sequential release is essential for invasion and the intracellular lifestyle of these eukaryotes. During invasion, rhoptries inject an array of invasion and virulence factors into the cytoplasm of the host cell, but the molecular mechanism mediating rhoptry exocytosis is unknown. Here we identify a set of parasite specific proteins, termed rhoptry apical surface proteins (RASP) that cap the extremity of the rhoptry. Depletion of RASP2 results in loss of rhoptry secretion and completely blocks parasite invasion and therefore parasite proliferation in both Toxoplasma and Plasmodium. Recombinant RASP2 binds charged lipids and likely contributes to assembling the machinery that docks/primes the rhoptry to the plasma membrane prior to fusion. This study provides important mechanistic insight into a parasite specific exocytic pathway, essential for the establishment of infection.

Date: 2019
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DOI: 10.1038/s41467-019-11979-z

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