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dc.contributor.authorKumpula, Esa-Pekkaen_US
dc.contributor.authorPires, Isaen_US
dc.contributor.authorLasiwa, Davkien_US
dc.contributor.authorPiirainen, Hennien_US
dc.contributor.authorBergmann, Ulrichen_US
dc.contributor.authorVahokoski, Juhaen_US
dc.contributor.authorKursula, Inarien_US
dc.PublishedKumpula E, Pires I, Lasiwa, Piirainen H, Bergmann U, Vahokoski J, Kursula I. Apicomplexan actin polymerization depends on nucleation. Scientific Reports. 2017;7:12137eng
dc.description.abstractFilamentous actin is critical for apicomplexan motility and host cell invasion. Yet, parasite actin filaments are short and unstable. Their kinetic characterization has been hampered by the lack of robust quantitative methods. Using a modified labeling method, we carried out thorough biochemical characterization of malaria parasite actin. In contrast to the isodesmic polymerization mechanism suggested for Toxoplasma gondii actin, Plasmodium falciparum actin I polymerizes via the classical nucleation-elongation pathway, with kinetics similar to canonical actins. A high fragmentation rate, governed by weak lateral contacts within the filament, is likely the main reason for the short filament length. At steady state, Plasmodium actin is present in equal amounts of short filaments and dimers, with a small proportion of monomers, representing the apparent critical concentration of ~0.1 µM. The dimers polymerize but do not serve as nuclei. Our work enhances understanding of actin evolution and the mechanistic details of parasite motility, serving as a basis for exploring parasite actin and actin nucleators as drug targets against malaria and other apicomplexan parasitic diseases.en_US
dc.publisherNature Publishing Groupeng
dc.rightsAttribution CC BYeng
dc.titleApicomplexan actin polymerization depends on nucleationen_US
dc.typePeer reviewed
dc.typeJournal article
dc.rights.holderCopyright 2017 The Author(s)
dc.source.journalScientific Reports

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