Neutralization of Toxic Heme by Plasmodium Falciparum Histidine-Rich Protein 2
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概要
- 論文の詳細を見る
Plasmodium falciparum histidine-rich protein 2 (PfHRP2) has been suggested to be an initiator of the polymerization of heme, which is produced as by-product on the digestion of hemoglobin, and a promoter of the H2O2-induced degradation of heme in food yacuoles of the malarial parasite. In this work, we have designed PfHRP2 model peptides, R18 and R27 (18 and 27 residues, respectively), and used them for optical and electron spin resonance spectroscopic measurements to confirm that the axial ligands of the heme-PfHRP2 complex are the nitrogenous donors derived from the imidazole moieties of histidine residues of PfHRP2. In addition, we revealed that the affinities of R18 and R27 for heme (Kd=2.21×10-6 M and 0.71×10-6M, respectively) might be as high as that of PfHRP2 (Kd=0.94×10-6M). The R27 peptide can remove heme from membrane-intercalated heme and inhibit heme-induced hemolysis. There-fore, we suggest another function of PfHRP2: it may play an important role in the neutralization of toxic heme in the parasite cytoplasm and infected erythrocytes by removing heme from heme-bound membranes or reducing heme-induced hemolysis.
- 社団法人 日本生化学会の論文
著者
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Huy Nguyen
Department Of Applied Biology Kyoto Institute Of Technology:department Of Immunogenetics Institute O
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Trang Dai
Department Of Applied Biology Kyoto Institute Of Technology
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Takano Ryo
Department Of Applied Biology Kyoto Institute Of Technology
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SERADA Satoshi
Department of Applied Biology, Kyoto Institute of Technology
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KONDO Yoshiro
Department of Applied Biology, Kyoto Institute of Technology
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Kanaori Kenji
Department Of Applied Biology Kyoto Institute Of Technology
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Tajima Kunihiko
Department Of Applied Biology Kyoto Institute Of Technology
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Hara Saburo
Department Of Applied Biology Kyoto Institute Of Technology
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Kamei Kaeo
Department of Applied Biology, Kyoto Institute of Technology
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