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Rifampicin resistance and mutation of the rpoB gene in Mycobacterium tuberculosis
Authors:Hatsumi Taniguchi  Hironori Aramaki  Yoshihiko Nikaido  yasuo Mizuguchi  Masahiro Nakamura  Toshihiko Koga  Shin-ichi Yoshida
Institution:Infection and Immunity, Institute of Biomedical and Life Sciences, Joseph Black Building, University of Glasgow, Glasgow G12 8QQ, UK; Department of Immunology, The Toad Centre, University of Strathclyde, Glasgow G4 0NR, UK; Animal Health Discovery, Pfizer Central Research, Sandwich, Kent CT13 9NJ, UK
Abstract:Abstract The bradyzoite and tachyzoite forms of Toxoplasma gondii , purified from infected animals, were analysed for their activities of phosphofructokinase, pyruvate kinase, lactate dehydrogenase, NAD+- and NADH-linked isocitrate dehydrogenases, and succinic dehydrogenase. Both developmental stages contained high activities of phosphofructokinase (specific for pyrophosphate rather than ATP), pyruvate kinase and lactate dehydrogenase, suggesting that energy metabolism in both forms may centre around a high glycolytic flux linked to lactate production. The markedly higher activity of the latter two enzymes in bradyzoites suggests that lactate production is particularly important in this developmental form. NAD+-specific isocitrate dehydrogenase was not detectable in either stage of the parasite (and proved useful as a measure of the purity of the bradyzoite preparation), whereas both parasite forms contained low activities of NADP+-linked isocitrate dehydrogenase. The results are consistent with the bradyzoites lacking a functional TCA cycle and respiratory chain and are suggestive of a lack of susceptibility of this developmental stage to atovaquone.
Keywords:Toxoplasma gondii            Tachyzoite  Bradyzoite  Enzymes  Glycolysis  Lactate dehydrogenase  TCA cycle
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