Molekylære mekanismer for parasittmotilitet


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open position

Post-doctoral (or graduate student) position in structural biology of parasite motility

We are looking for a post-doctoral fellow for a 2.5-year project (possible extension for up to 1 year) in my group at the Faculty of Biochemistry and Molecular Medicine (FBMM), University of Oulu, Finland. Alternatively, an exceptionally highly-qualified PhD student could be considered. The overall aim of my group is to understand the molecular mechanism of malaria parasite gliding motility. To reach this goal, we use a wide variety of structural biology and biochemical/biophysical methods. Our ongoing work is focused on (i) the polymerization and ATPase mechanism of actin, (ii) parasite actomyosin complexes, (iii) the structure and function of the glideosome-associated linker protein, and (iv) reconstructing the entire membrane-delimited motor complex in vitro for structural and functional studies. The exact project will be agreed upon based on the experience and interests of the successful candidate.

group picture
Seija Leskelä


The candidate should have a PhD (or MSc if applying for a graduate student position) in a relevant field of science and have experience, or at least a keen interest, in all or several of the following:

- molecular biology and protein expression and purification

- biophysical and biochemical characterization of proteins and their complexes

- protein crystallography and/or cryo-EM

- light and/or electron microscopy

We welcome applications particularly from candidates willing and eligible to apply for competitive funding from national, European, and international sources.

Our research group is split between the FBMM in Oulu and the Department of Biomedicine, University of Bergen, Norway. Our laboratories and the available core facilities available have state-of-the-art equipment for molecular biology, protein biochemistry/biophysics, and electron and light microscopy. We have active collaborations for cryo-EM and cell biology/parasitology.

The project is funded by the Sigrid Jusélius foundation, and the candidate will receive a personal stipend (tax-exempt up to the limit defined by the Finnish tax authorities and subject to a compulsory pension insurance).

Informal inquiries and applications including a motivation letter, a CV with publication list, and contact information for 2-3 referees are to be sent to inari.kursula@oulu.fi. Applications will be considered until a suitable candidate has been identified. The starting date is as soon as possible.

Publications most relevant for the project:

Pires I, Hung YF, Bergmann U, Molloy JE & Kursula I (2022) Analysis of Plasmodium falciparum myosin B ATPase activity and structure in complex with the calmodulin-like domain of its light chain MLC-B. J Biol Chem in press, https://doi.org/10.1016/j.jbc.2022.102634

Vahokoski J, Calder L, Lopez AJ, Molloy JE, Kursula I & Rosenthal PB (2022) High-resolution structures of malaria parasite actomyosin and actin filaments. PLoS Pathog 18: e1010408.

Kumpula EP, Lopez AJ, Tajedin L, Han H & Kursula I (2020) Atomic view into Plasmodium actin polymerization, ATP hydrolysis, and fragmentation. PLoS Biol 17: e3000315.

Kumpula EP, Pires IP, Lasiwa D, Piirainen H, Bergmann U, Vahokoski J & Kursula I (2017) Apicomplexan actin polymerization depends on nucleation. Sci Rep 7: 12137.

Pospich S, Kumpula EP, von der Ecken J, Vahokoski J, Kursula I & Raunser S (2017) Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability. Proc Natl Acad Sci USA 114: 10636-10641.

Jacot D, Tosetti N, Pires IP, Stock J, Graindorge A, Hung YF, Han H, Tewari R, Kursula I & Soldati-Favre D (2016) An apicomplexan actin-binding protein serves as a connector and lipid sensor to coordinate motility and invasion. Cell Host Microbe 20: 731-743.

More info:

Group webpages in Oulu and Bergen

Selected publications