Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 432, Issue 4, Pages 878-896Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2019.12.024
Keywords
malaria; plasmodium; host cell invasion; armadillo proteins; BioID
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Funding
- Canadian Institutes of Health Research [MOP-89903]
- DAAD/Universities Australia
- Joachim Herz Foundation
- NHMRC [APP1143974]
- University of Adelaide Beacon Fellowships
- ARC PhD Scholarship
- German Research Foundation (DFG) [BA 5213/3-1]
- EMBL Interdisciplinary Postdoc (EIPOD) program under Marie Sklodowska-Curie Actions COFUND program [664726]
- Joachim Herz Stiftung Add-on Fellowship for Interdisciplinary Sciences [850016]
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Apicomplexan parasites contain rhoptries, which are specialized secretory organelles that coordinate host cell invasion. During the process of invasion, rhoptries secrete their contents to facilitate interaction with, and entry into, the host cell. Here, we report the crystal structure of the rhoptry protein Armadillo Repeats-Only (ARO) from the human malaria parasite, Plasmodium falciparum (PfARO). The structure of PfARO comprises five tandem Armadillo-like (ARM) repeats, with adjacent ARM repeats stacked in a head-to-tail orientation resulting in PfARO adopting an elongated curved shape. Interestingly, the concave face of PfARO contains two distinct patches of highly conserved residues that appear to play an important role in protein-protein interaction. We functionally characterized the P. falciparum homolog of ARO interacting protein (PfAIP) and demonstrate that it localizes to the rhoptries. We show that conditional mislocalization of PfAIP leads to deficient red blood cell invasion. Guided by the structure, we identified mutations of PfARO that lead to mislocalization of PfAIP. Using proximity-based biotinylation we probe into PfAIP interacting proteins. (C) 2019 Published by Elsevier Ltd.
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