Pyruvate kinase type-II isozyme in Plasmodium falciparum localizes to the apicoplast

Takuya Maeda, Tomoya Saito, Omar S. Harb, David S. Roos, Satoru Takeo, Hiroko Suzuki, Takafumi Tsuboi, Tsutomu Takeuchi, Takashi Asai

研究成果: Article査読

25 被引用数 (Scopus)


Bioinformatics research on Plasmodium falciparum revealed two isoforms of pyruvate kinase: type-I and type-II enzymes. The type-I enzyme shows typical glycolytic properties, while type-II enzyme is involved in fatty acid type-II biosynthesis and has been predicted to localize to the apicoplast with the targeting signal in its N-terminus. The type-I and type-II isoforms have the same evolutionary origin as Toxoplasma gondii isozymes, TgPyKI and TgPyKII, respectively; however, TgPyKII localizes to both the mitochondrion and the apicoplast. Accordingly, we made a recombinant full length of P. falciparum pyruvate kinase type-II protein using a wheat germ cell-free expression system and obtained a specific antibody against the type-II protein. Fluorescent microscopic analysis revealed that P. falciparum type-II enzyme was localized only to the apicoplast, not to the mitochondrion. The data suggest differences in localization and metabolic pathways between P. falciparum and T. gondii pyruvate kinase isoforms.

ジャーナルParasitology International
出版ステータスPublished - 2009 3月

ASJC Scopus subject areas

  • 寄生虫科
  • 感染症


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