title: Babesia gibsoni-specific isoenzymes related to energy metabolism of the parasite in infected erythrocytes.
abstract: To clarify the cause of the predilection of Babesia gibsoni for reticulocytes and canine HK erythrocytes (containing high concentrations of potassium) with inherited high concentrations of some amino acids, including glutamate, 4 enzymes in B. gibsoni parasites were examined by polyacrylamide gel electrophoresis (PAGE). The enzymes, i.e., hexokinase, glucose phosphate isomerase, lactate dehydrogenase, and glutamate dehydrogenase (GDH), were found to be associated with B. gibsoni parasites. The parasite-specific enzymes were shown to have different mobility patterns in PAGE from those found in normal canine erythrocytes. GDH, which is able to oxidize glutamate to alpha-ketoglutarate, an intermediate in the citric acid cycle in mitochondria, was detected only in the parasites. Electron microscopy of the parasites revealed double-membraned organelles similar to mitochondria in their cytoplasm. The parasites in in vitro culture contained many more mitochondrialike organelles than those in the peripheral blood of infected dogs. In addition, the size of parasites cultured in vitro was significantly larger than that of parasites in the peripheral blood. Based on these results, it is suggested that B. gibsoni may use glucose as an energy source in its own glycolytic pathway. Moreover, the parasite may also be capable of oxidizing glutamate via GDH in the citric acid cycle, which may operate in the mitochondrialike organelles within the parasite. This may explain the predilection of B. gibsoni for canine reticulocytes and HK erythrocytes with a high concentration of glutamate.
authors.affiliation: Laboratory of Internal Medicine, Department of Veterinary Medical Sciences, Graduate School of Hokkaido University, Sapporo 060-0818, Japan.
authors.forename: Masahiro
authors.initials: M
authors.lastname: Yamasaki
authors.forename: Mohammad Alamgir
authors.initials: MA
authors.lastname: Hossain
authors.forename: Ja-Ryong
authors.initials: JR
authors.lastname: Jeong
authors.forename: Hye-Sook
authors.initials: HS
authors.lastname: Chang
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Satoh
authors.forename: Osamu
authors.initials: O
authors.lastname: Yamato
authors.forename: Yoshimitsu
authors.initials: Y
authors.lastname: Maede
mesh_terms: D000818:Animals; D001403:Babesia / Q000201:enzymology* / Q000378:metabolism / Q000648:ultrastructure; D002478:Cells, Cultured; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D004734:Energy Metabolism / Q000502:physiology*; D004912:Erythrocytes / Q000378:metabolism / Q000469:parasitology* / Q000648:ultrastructure; D005956:Glucose-6-Phosphate Isomerase / Q000032:analysis / Q000502:physiology; D005969:Glutamate Dehydrogenase / Q000032:analysis / Q000502:physiology; D006593:Hexokinase / Q000032:analysis / Q000502:physiology; D007527:Isoenzymes / Q000032:analysis / Q000502:physiology*; D007770:L-Lactate Dehydrogenase / Q000032:analysis / Q000502:physiology; D008854:Microscopy, Electron
chemical_list: D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase; D005969:Glutamate Dehydrogenase; D006593:Hexokinase; D005956:Glucose-6-Phosphate Isomerase