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|Title:||Structural insights into PfARO and characterization of its interaction with PfAIP|
|Citation:||Journal of Molecular Biology, 2020; 432(4):878-896|
|Michael Geiger, Chris Brown, Jan Stephan Wichers, Jan Strauss, Andrés Lill, Roland Thuenauer, Benjamin Liffner, Louisa Wilcke, Sarah Lemcke, Dorothee Heincke, Samuel Pazicky, Anna Bachmann, Christian Löw, Danny William Wilson, Michael Filarsky, Paul-Christian Burda, Kun Zhang, Murray Junop, and Tim Wolf Gilberger|
|Abstract:||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 is comprised of 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 homologue 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.|
|Keywords:||Malaria; plasmodium; host cell invasion; armadillo proteins; BioID|
|Rights:||© 2019 Published by Elsevier Ltd.|
|Appears in Collections:||Microbiology and Immunology publications|
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