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Babesia bovis Dihydroorotate Dehydrogenase (BboDHODH) is a Novel Molecular Target of Drug for Bovine Babesiosis OAK
KAMYINGKIRD, Ketsarin; CAO, Shinuo; MASATANI, Tatsunori; MOUMOUNI, Paul Franck Adjou; VUDRIKO, Patrick; MOUSA, Ahmed Abd El Moniem; TERKAWI, Mohamad Alaa; NISHIKAWA, Yoshifumi; IGARASHI, Ikuo; XUAN, Xuenan; 西川, 義文; 五十嵐, 郁男; 玄, 学南.
The emergence of drug resistance and adverse side effects of current bovine babesiosis treatment suggest that the search of new drug targets and development of safer and effective compounds are required. This study focuses on dihydroorotate dehydrogenase (DHODH), the fourth enzyme of pyrimidine biosynthesis pathway as a potential drug target for bovine babesiosis. Recombinant Babesia bovis DHODH protein (rBboDHODH) was produced in Escherichia coli and used for characterization and measurement of enzymatic activity. Furthermore, the effects of DHODH inhibitors were evaluated in vitro. The recombinant B. bovis DHODH histidine fusion protein (rBboDHODH) had 42.4-kDa molecular weight and exhibited a specific activity of 475.7 ± 245 Unit/mg, a Km = 276.2 µM for...
Palavras-chave: Atovaquone; Babesia bovis; Chemotherapeutic target agent; Dihydroorotate dehydrogenase; Leflunomide.
Ano: 2014 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/3918
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