Abstract:
:Plasmodium parasites are obligate intracellular protozoa and causative agents of malaria, responsible for half a million deaths each year. The lifecycle progression of the parasite is reliant on cell motility, a process driven by myosin A, an unconventional single-headed class XIV molecular motor. Here we demonstrate that myosin A from Plasmodium falciparum (PfMyoA) is critical for red blood cell invasion. Further, using a combination of X-ray crystallography, kinetics, and in vitro motility assays, we elucidate the non-canonical interactions that drive this motor's function. We show that PfMyoA motor properties are tuned by heavy chain phosphorylation (Ser19), with unphosphorylated PfMyoA exhibiting enhanced ensemble force generation at the expense of speed. Regulated phosphorylation may therefore optimize PfMyoA for enhanced force generation during parasite invasion or for fast motility during dissemination. The three PfMyoA crystallographic structures presented here provide a blueprint for discovery of specific inhibitors designed to prevent parasite infection.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Robert-Paganin J,Robblee JP,Auguin D,Blake TCA,Bookwalter CS,Krementsova EB,Moussaoui D,Previs MJ,Jousset G,Baum J,Trybus KM,Houdusse Adoi
10.1038/s41467-019-11120-0subject
Has Abstractpub_date
2019-07-23 00:00:00pages
3286issue
1issn
2041-1723pii
10.1038/s41467-019-11120-0journal_volume
10pub_type
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