molecular mechanisms of actin-based motility


Cytoskeletal proteins recognize and bind to each other. Actin - the central protein of the cytoskeleton - polymerizes to form complex structures together with other components of the cytoskeleton and various regulatory proteins. Pathogens use these cytoskeletal complexes for both motility and invasion of their host cells. Once these mechanisms are understood at the molecular - or atomic - level, we can look for ways to interfere with the processes of motility and invasion.

We study the motility and host cell invasion of the parasite causing malaria, which is one of the world's most devastating infectious diseases. Each year, more than a million people die of malaria. The disease is caused by Plasmodium spp., which comprise a group of unicellular, eukaryotic, intracellular parasites. They use actin for motility and invasion of host cells but their cytoskeleton differs markedly from that of higher eukaryotes. Actin filaments of Plasmodium and related parasites are extremely short, and their rapid treadmilling is regulated by a strikingly small number of actin-binding proteins.

It is these proteins that are in the limelight of our research group: How do the three-dimensional structures of these proteins look like? What do the complexes they form look like and how do they work? How can we interfere with their function? Answers to these questions can be found by means of X-ray crystallography and small-angle X-ray scattering, combined with other biophysical and biochemical methodology. We aim to shed light on the structure and function of these proteins and complexes, using new methods based on the accelerator technologies at DESY: making large structures of the cytoskeleton visible - at high resolution - using most modern synchrotron radiation sources.


Helmholtz Centre for Infection Research


Hamburg, Germany

Faculty of Biochemistry and

Molecular Medicine

University of Oulu

Oulu, Finland

Department of Biomedicine

University of Bergen

Bergen, Norway