Molecular characterization of the glutathione peroxidase gene of the human malaria parasite Plasmodium falciparum

• Published in: Molecular and biochemical parasitology Vol. 78; no. 1-2; pp. 237 - 248
• Main Authors: Gamain, Benoît, Langsley, Gordon, Fourmaux, Marie N., Touzel, Jean P., Camus, Daniel, Dive, Daniel, Slomianny, Christian
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.06.1996; Elsevier
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Binding Sites - genetics; Chemical and Process Engineering; DNA, Protozoan - genetics; Engineering Sciences; Food engineering; Gene; Genes, Protozoan; Glutathione peroxidase; Glutathione Peroxidase - chemistry; Glutathione Peroxidase - genetics; Glutathione Peroxidase - metabolism; Humans; Introns; Life Sciences; Malaria; Molecular Sequence Data; Molecular Structure; Molecular Weight; Nucleic Acid Conformation; Phylogenetic tree; Phylogeny; Plasmodium falciparum; Plasmodium falciparum - enzymology; Plasmodium falciparum - genetics; Polymerase Chain Reaction; RNA, Protozoan - chemistry; RNA, Protozoan - genetics; Selenium; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Species Specificity; Glutathione peroxidase; PhGPx; Plasmodium falciparum; Malaria; Gene; Phylogenetic tree; ROS; SOD; Selenium; GPx; PCR; PfGPx; GLUTATHIONE PEROXIDASE; MALARIA
• ISSN: 0166-6851; 1872-9428
• DOI: 10.1016/S0166-6851(96)02632-1

In this paper we report the isolation and the characterization of a gene encoding the antioxidant enzyme glutathione peroxidase from the human malaria parasite Plasmodium falciparum. This gene contains two introns of 208 and 168 bp and is present in a single copy on chromosome 13. The open reading frame encodes a protein with a predicted length of 205 amino acids, which possesses a potential cleavage site between residues 21 and 22 after a hydrophobic region with the characteristics of a signal sequence. Therefore, the mature protein is predicted to be 184 residues long with a molecular mass of 21 404 Da. In comparison with other known glutathione peroxidases many amino acid residues implicated in catalysis are conserved in the malarial enzyme. Phylogenetic analysis indicates that the deduced protein sequence is more closely related to plant glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase. A 1.5-kb transcript was identified in asynchronous erythrocytic stages.