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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/40708
Title: Characterization of Plasmodium falciparum ATP-dependent DNA helicase RuvB3
Authors: Paviga Limudomporn
Saengduen Moonsom
Ubolsree Leartsakulpanich
Pattra Suntornthiticharoen
Songsak Petmitr
Michael Weinfeld
Porntip Chavalitshewinkoon-Petmitr
Mahidol University
Thailand National Center for Genetic Engineering and Biotechnology
Rangsit University
University of Alberta
Keywords: Immunology and Microbiology;Medicine
Issue Date: 3-Nov-2016
Citation: Malaria Journal. Vol.15, No.1 (2016), 1-10
Abstract: © 2016 The Author(s). Background: Malaria is one of the most serious and widespread parasitic diseases affecting humans. Because of the spread of resistance in both parasites and the mosquito vectors to anti-malarial drugs and insecticides, controlling the spread of malaria is becoming difficult. Thus, identifying new drug targets is urgently needed. Helicases play key roles in a wide range of cellular activities involving DNA and RNA transactions, making them attractive anti-malarial drug targets. Methods: ATP-dependent DNA helicase gene (PfRuvB3) of Plasmodium falciparum strain K1, a chloroquine and pyrimethamine-resistant strain, was inserted into pQE-TriSystem His-Strep 2 vector, heterologously expressed and affinity purified. Identity of recombinant PfRuvB3 was confirmed by western blotting coupled with tandem mass spectrometry. Helicase and ATPase activities were characterized as well as co-factors required for optimal function. Results: Recombinant PfRuvB3 has molecular size of 59 kDa, showing both DNA helicase and ATPase activities. Its helicase activity is dependent on divalent cations (Cu2+, Mg2+, Ni+2 or Zn+2) and ATP or dATP but is inhibited by high NaCl concentration (>100 mM). PfPuvB3 is unable to act on blunt-ended duplex DNA, but manifests ATPase activity in the presence of either single- or double-stranded DNA. PfRuvB3.is inhibited by doxorubicin, daunorubicin and netropsin, known DNA helicase inhibitors. Conclusions: Purified recombinant PfRuvB3 contains both DNA helicase and ATPase activities. Differences in properties of RuvB between the malaria parasite obtained from the study and human host provide an avenue leading to the development of novel drugs targeting specifically the malaria form of RuvB family of DNA helicases.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84994049811&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/40708
ISSN: 14752875
Appears in Collections:Scopus 2016-2017

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