Master of Science Esa-Pekka Kumpula
Faculty and research unit
University of Oulu Graduate School, Faculty of Biochemistry and Molecular Medicine, Molecular mechanisms of parasite motility
Field of study
Structural biology, biochemistry
Date and time of the thesis defence
Place of the thesis defence
Aapistie 7A, lecture hall F101
Topic of the dissertation
Elucidation of Strucure-Function Relationships in Malaria Parasite Actins
Professor Yuichiro Maéda, Nagoya University, Japan
Professor Inari Kursula, University of Oulu, Faculty of Biochemistry and Molecular Medicine and University of Bergen, Department of Biomedicine
Structure of the Protein Actin from the Malaria Parasite
The present PhD study focused on finding out the mechanism that defines the short length of malaria parasite actin filaments. The main technique of study was structural work based on structures of the protein at the atomic level. At the moment, high resolution information of the molecular machinery that allows parasite movement is scarce. This machinery is necessary for the survival of the parasite and understanding its structure at the atomic level opens up new avenues for drug development.
Actin is a filament-forming structural protein found in all animals, plants and fungi. It has a central role in many processes in the human body, including muscle contraction and cell division. Actins from humans and other mammals have been extensively studied and the differences between species are minimal. However, differences to malaria parasite actin are significant, so information extracted from mammalian actins cannot be directly applied to malaria parasite actins. On the other hand, these differences allow design of drugs that specifically target malaria parasite actins and not human actins. In this work, a significant amount of structural information was extracted and analyzed from malaria parasite actins. Using this information, an atomic level mechanism was presented that explains their unusually short filament length.
Last updated: 5.4.2019