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Subcellular localization of some glycolytic enzymes in parasitic flagellated protozoa.

1. The glycolytic enzymes of Tritrichomonas foetus, unlike those of Trypanosoma brucei, are apparently not located in microbody-like organelles (glycosomes) but appear to occur in the cytosol. 2. The localization of the glycolytic enzymes in Crithidia fasciculata and in the epimastigote and trypomastigote forms of Trypanosoma cruzi is however similar to that in T. brucei. 3. No evidence was obtained for the existence of glycolytic enzyme-containing microbodies in rat liver. 4. The glycosome is probably an organelle unique to members of the Kinetoplastida.

Animals↗

Effects of the intestinal flagellate, Cochlosoma anatis, on intestinal mucosal morphology and disaccharidase activity in Muscovy ducklings.

Newly hatched female Muscovy ducklings were randomly separated into 2 groups of 12 and 1 group of 13. Ducklings in the first 2 groups were each orally inoculated with 0.5 ml of sterile normal saline containing 0 and 3 x 10(6) trophozoites of Cochlosoma anatis, respectively. Birds in the third group were each orally inoculated with 3 x 10(6) trophozoites for 5 consecutive days. Birds were weighed daily for the first 5 days and then on days 7, 14 and 21 post-inoculation (p.i.). On days 6, 7, 8, 13, 14, 15, 20, 21 and 22 p.i., 1 bird from each group was killed and samples of intestine at 7 levels were taken for trophozoite counts, mucosal disaccharidase analyses and morphometric analysis. Body weights did not differ among treatment groups at any time during the experiment. Trophozoite numbers did not change over the period 6-22 days p.i. Trophozoite numbers were lowest in the anterior small intestine and increased distally, but very few were observed in the caecum. Crypt depth was greater in all regions of the small intestine in inoculated groups compared to uninoculated controls, and was significantly increased in the duodenum, proximal jejunum and mid-jejunum (P < 0.05). Villus height was greater in inoculated groups compared to controls at all levels of the intestine and was significantly increased in the duodenum, proximal jejunum and ileum (P < 0.05). Mucosal palatinase and maltase activity in the small intestine were reduced in inoculated groups compared to uninoculated controls; palatinase activities were significantly reduced in the proximal and mid-jejunum and maltase activities were significantly reduced in the mid-jejunum (P < 0.05). Sucrase activities were significantly increased at all levels of the small intestine in inoculated ducklings compared to uninoculated controls (P < 0.05). Although no clinical signs were evident, Cochlosoma infection significantly altered intestinal morphometrics and mucosal enzyme concentrations in ducklings, in several cases in a counter-intuitive direction.

Animals↗

The in vivo and in vitro action of 4-amino-5-imidazolecarboxamide in trypanosomatid flagellates.

4-Amino-5-imidazolecarboxamide, but not its riboside or ribotide, is inhibitory to the growth of promastigotes of Leishmania donovani, L. braziliensis, L. tarentolae, and L. mexicana, eventually causing cell lysis. Conversely, it is not inhibitory to the growth of epimastigotes of Trypanosoma cruzi. This substituted imidazole proved to be an excellent inhibitor of guanine deaminase from all of the trypanosomatids used in this study, with Ki values in the microM range.

Aminoimidazole Carboxamide↗

The pathway of arginine catabolism in the parasitic flagellate Trichomonas vaginalis.

Arginine is rapidly depleted from the medium during the cultivation of T. vaginalis in a defined or semi-defined medium. It is broken down to ornithine, ammonia and carbon dioxide by the three enzymes of the dihydrolase pathway: arginine deiminase, catabolic ornithine carbamyltransferase (OCTase) and carbamate kinase. Arginase and urease as well as citrulline hydrolase appear to be absent. Ornithine, a product of the pathway was further converted to putrescine by an active ornithine decarboxylase. Apparent substrate Km values determined were arginine deiminase, 103 microM; catabolic OCTase, 71 microM; ornithine decarboxylase 134 microM. A substrate level phosphorylation is associated with the pathway; the significance of this to the overall energy economy of the cell is unclear.

Adenosine Diphosphate↗

Conservative and divergent base sequence regions in the maxicircle kinetoplast DNA of several trypanosomatid flagellates.

The structure of kinetoplast maxicircle DNA from trypanosomatids Crithidia oncopelti, C. luciliae, Leptomonas pessoai and Leishmania gymnodactyli was compared by the blot hybridization method. The sizes of these molecules are 24.5, 34, 31 and 38 kilobase pairs (kbp), respectively. Labelled maxicircle fragments from C. oncopelti were used as probes. A general model of the structural organization of maxicircles is proposed according to which this molecule is composed of a 17kbp conservative region and a divergent one occupying the rest of the molecule. The conservative region contains the sequences homologous to those in all trypanosomatids. The sequence of the divergent region exhibits no cross homology detectable by high stringency hybridization. The main size differences between the maxicircle molecules from different trypanosomatid species are explained by the length variability of their divergent regions.

Animals↗