Elucidation of Strucure-Function Relationships in Malaria Parasite Actins

Thesis event information

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

Doctoral candidate

Master of Science Esa-Pekka Kumpula

Faculty and unit

University of Oulu Graduate School, Faculty of Biochemistry and Molecular Medicine, Molecular mechanisms of parasite motility

Subject of study

Structural biology, biochemistry

Opponent

Professor Yuichiro Maéda, Nagoya University, Japan

Custos

Professor Inari Kursula, University of Oulu, Faculty of Biochemistry and Molecular Medicine and University of Bergen, Department of Biomedicine

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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