Inari Kursula lab

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A red cartoon representation of an actin monomer and a b/w surface view of an actin filament on a yellow background of negatively stained actin filaments.

Molecular mechanisms of parasite motility

Malaria is one of the world's most devastating infectious diseases. Each year, nearly half a million people die of malaria. The disease is caused by Plasmodium spp., which comprise a group of unicellular, eukaryotic, intracellular parasites, belonging to the phylum Apicomplexa. They use an actomyosin motor complex, termed glideosome, for rapid gliding motility and host cell invasion. The motor components are to a large extent unique to these parasites or highly diverged from the corresponding human proteins. Parasite actin filaments are short, and their rapid treadmilling is regulated by an unusually small number of actin-binding proteins.

Our work is focused on understanding malaria parasite gliding motility and the molecular machinery behind at the molecular/atomic level. A broad range of structural biology and biochemical/biophysical methods is used for this aim.

Our work is aimed at a mechanistic understanding of gliding motility, which malaria parasites and their relatives use for getting to and invading their host cells. We employ a broad range of biochemical, biophysical and hybrid structural biology methods for creating a complete molecular picture of the parasite actin-myosin motor and the entire glideosome. We also want to understand the evolution of apicomplexan gliding motility and eukaryotic actin-myosin motors in a broader sense. Understanding the mechanistic differences in cell motility between parasites and humans may, furthermore, open up new avenues for treatment and/or prevention of malaria.

We have determined atomic structures of malaria parasite actins in both monomeric and filamentous form and characterized their polymerization properties as well as nearly all the parasite actin-binding proteins known to date. Our future work is directed more towards larger complexes and reconstructing the entire parasite glideosome for structural and functional characterization.

My research group is divided between the Faculty of Biochemistry and Molecular Medicine at the University of Oulu, Finland, and the Department of Biomedicine, University of Bergen, Norway.

paper in press
Actin II structure

Paper on Plasmodium actin II accepted for publication

Andrea's paper on the structure and cellular localization of malaria parasite actin II was accepted for publication in PLoS Pathogens today! The work was a huge long-term collaborative effort between our lab and the lab of Inga Sidén-Kiamos at IMBB-FORTH, Heraklion, Crete, and that of Peter...

New preprint
GAC structure

Surprising structure of Toxoplasma gondii GAC

After years of work, we finally can see what the apicomplexan glideosome-associated connector (GAC) really looks like! Check out our latest preprint presenting the structure in two drastically different conformations. Based on its structure, we suggest a role for GAC as an elastic spring helping...

New preprint
preprint ad

Check out our latest work on actin II

Andrea's work together with collaborators from IMBB-FORTH (Heraklion, Crete) and Francis Crick Institute (London, UK) on malaria parasite actin II is out in preprint form.

bioRxiv title page

Check out our latest preprint on targeting malaria parasite profilactin with drugs

Henni's recent work on characterizing compounds interfering with the malaria parasite profilin-actin complex and actin dynamics is out as a preprint on bioRxiv. The project is part of a large collaboration led by Madeline Dans and Paul Gilson from the Burnet Institute, Melbourne, Australia.

Guest speaker
Linda on the top of Ulriken

Today's guest is Linda Sandblad from Umeå

Today, we have a special pleasure to host Dr. Linda Sandblad, the Director of the Umeå Centre for Electron Microscopy, as our BBB seminar speaker. Already visited Ulriken to see Bergen from above and had exciting exchange of ideas on our projects. Now looking forward to Linda's talk at 14:30. Come...

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