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J Biol Chem. 2017 Oct 27;292(43):17857-17875. doi: 10.1074/jbc.M117.802769. Epub 2017 Sep 11.

Compositional and expression analyses of the glideosome during the Plasmodium life cycle reveal an additional myosin light chain required for maximum motility.

Author information

From the Malaria Parasitology Laboratory,
the School of Life Sciences, Queens Medical Centre, University of Nottingham, Nottingham NG7 2UH, United Kingdom.
the Department of Biomedicine, University of Bergen, Jonas Lies vei 91, 5009 Bergen, Norway.
From the Malaria Parasitology Laboratory.
the Institute of Cell Biology, University of Bern, Bern, Switzerland, and.
Structural Biology and.
Mass Spectrometry Science Technology Platforms, and.
the Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Aapistie 7, 90220 Oulu, Finland.
Single Molecule Enzymology Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, United Kingdom.
From the Malaria Parasitology Laboratory,


Myosin A (MyoA) is a Class XIV myosin implicated in gliding motility and host cell and tissue invasion by malaria parasites. MyoA is part of a membrane-associated protein complex called the glideosome, which is essential for parasite motility and includes the MyoA light chain myosin tail domain-interacting protein (MTIP) and several glideosome-associated proteins (GAPs). However, most studies of MyoA have focused on single stages of the parasite life cycle. We examined MyoA expression throughout the Plasmodium berghei life cycle in both mammalian and insect hosts. In extracellular ookinetes, sporozoites, and merozoites, MyoA was located at the parasite periphery. In the sexual stages, zygote formation and initial ookinete differentiation precede MyoA synthesis and deposition, which occurred only in the developing protuberance. In developing intracellular asexual blood stages, MyoA was synthesized in mature schizonts and was located at the periphery of segmenting merozoites, where it remained throughout maturation, merozoite egress, and host cell invasion. Besides the known GAPs in the malaria parasite, the complex included GAP40, an additional myosin light chain designated essential light chain (ELC), and several other candidate components. This ELC bound the MyoA neck region adjacent to the MTIP-binding site, and both myosin light chains co-located to the glideosome. Co-expression of MyoA with its two light chains revealed that the presence of both light chains enhances MyoA-dependent actin motility. In conclusion, we have established a system to study the interplay and function of the three glideosome components, enabling the assessment of inhibitors that target this motor complex to block host cell invasion.


cell motility; glideosome; invasion; malaria; myosin; myosin light chain; plasmodium

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