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J. Biochem, 2003, Vol. 133, No. 5 693-698
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Neutralization of Toxic Heme by Plasmodium Falciparum Histidine-Rich Protein 2

Nguyen Tien Huy, Satoshi Serada, Dai Thi Xuan Trang, Ryo Takano, Yoshiro Kondo, Kenji Kanaori, Kunihiko Tajima, Saburo Hara and Kaeko Kamei+

Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585

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 vacuoles 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 x 10–6 M and 0.71 x 10–6 M, respectively) might be as high as that of PfHRP2 (Kd = 0.94 x 10–6 M). The R27 peptide can remove heme from membrane-intercalated heme and inhibit heme-induced hemolysis. Therefore, 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.

+ To whom correspondence should be addressed. Tel: +81-75-724-7553, Fax: +81-75-724-7532, E-mail: kame{at}ipc.kit.ac.jp


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