Cloning, expression and functional activity of deoxyhypusine synthase from Plasmodium vivax |
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Authors: | James T Njuguna Marwa Nassar Achim Hoerauf Annette E Kaiser |
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Affiliation: | (1) Institute for Medical Microbiology, Immunology and Parasitology, D-53105 Bonn, Germany;(2) International Livestock Research Institute (ILRI), Naivasha road, P.O. Box 30709, Nairobi, Kenya;(3) Theodor Bilharz Research Institute, Warak El-Hadar, Kornish El Nile, P.O. Box 30 Imbaba, 12411 Giza, Egypt;(4) The German University in Cairo, Main Entrance of Al Tagamoa Al Khames, New Cairo City, Egypt |
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Abstract: | Background Plasmodium vivax is the most widespread human malaria parasite. However, genetic information about its pathogenesis is limited at present, due to the lack of a reproducible in vitro cultivation method. Sequencing of the Plasmodium vivax genome suggested the presence of a homolog of deoxyhypusine synthase (DHS) from P. falciparum, the key regulatory enzyme in the first committed step of hypusine biosynthesis. DHS is involved in cell proliferation, and thus a valuable drug target for the human malaria parasite P. falciparum. A comparison of the enzymatic properties of the DHS enzymes between the benign and severe Plasmodium species should contribute to our understanding of the differences in pathogenicity and phylogeny of both malaria parasites. |
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