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- Most-booked hotels in Palmas in the past month
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- Sensitivity of the Dengue Surveillance System in Brazil for Detecting Hospitalized Cases.
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Excelente pra quem pretende fazer Compras! Google Translation. Bem localizado. Date of stay: November Value. Helpful Share. Write your review. Share your best travel photo. Get quick answers. Not the right property for you? See all properties. Brazil State of Goias Goiania. Is This Your Tripadvisor Listing? Claim Your Listing. Frequently Asked Questions about Hotel Contorno. Which popular attractions are close to Hotel Contorno? Nearby attractions include Teatro Madre Esperanca Garrido 0. See all nearby attractions. What are some of the property amenities at Hotel Contorno?
Some of the more popular amenities offered include free wifi, airport transportation, and room service. See all property amenities. See all nearby restaurants. Yes, Hotel Contorno offers an airport shuttle for guests. We recommend calling ahead to confirm details. Learn more. Are there any historical sites close to Hotel Contorno? A minimum of cells on each microscope slide were used to evaluate fluorescence intensity in triplicate. The software determined the fluorescence intensity in pixels and standard error of each analysis. The survival of the Paracoccidioides isolates was determined by quantifying the number of colony-forming units CFUs recovered from macrophage infection.
J 1. Macrophages were lysed with water and fungal cells were recovered. The number of viable cells was determined based on the number of CFUs. Data were expressed as the mean value deviation from triplicate measurements and the statistical analyses were performed using ANOVA.
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To determine the adequate time of exposure of the isolates to sodium acetate for the proteomic assays, the enzymatic activity of ICL was determined in the four isolates at different time intervals 18, 24, 48, and 72 h. ICL and other enzymes of the glyoxylate cycle are induced under conditions such as low glucose levels and low oxygen tension Wayne and Lin, ; Fernandez et al. The enzymatic activity of ICL was reduced when glucose was used as a carbon source in relation to acetate in yeast cells of P.
Isocitrate lyase ICL activity assay. Activity was determined by measuring the formation of glyoxylate as its phenylhydrazone derivative under each condition. A total of 50 mg of each total protein extract of Paracoccidioides isolates Pb 01, Pb 03, Pb , and Pb EPM83 yeast cells were cultivated in minimal media with sodium acetate mM and glucose mM for different times 18, 24, 48, and 72 h.
Yeast cells of P. Growth was evaluated by dry weight analysis at several time intervals. For all isolates, growth was significantly reduced in the presence of sodium acetate compared to glucose, as depicted in Supplementary Figure 1. The lower growth in acetate likely reflects the lower content of proteins extracted under this condition, as follows: Pb 01 glucose Similar results were observed in Escherichia coli grown on acetate or glucose Treitz et al.
We identified differentially expressed proteins among P. The proteins identified in the four analyzed groups of the genus Paracoccidioides are depicted in Supplementary Table 1.
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A total of 1,, 1,, 1,, and 1, proteins were identified in P. The proteins in each isolate that grew in the presence of acetate were compared to the counterparts in yeast cells growing in the presence of glucose. Statistical analysis revealed differential protein expression in each isolate in relation to the carbon source used. Based on the differential protein expression results, the different isolates were compared using the heat map.
There were , , , and differentially expressed proteins showing fold-changes of at least 1. The number of differentially expressed proteins when comparing the four isolates to the others were These data indicate that high metabolic flexibility exists among members of the Paracoccidioides genus. Similar results were observed by Pigosso et al. Based on statistical analysis, the differentially expressed proteins were classified.
Supplementary Tables 2 — 9 present the proteins of the analyzed isolates significantly up- or down-regulated upon growth with the two-carbon molecule acetate. Those proteins were classified according to the functional categories present in FunCat2. The functional categories for up- and down-regulated proteins were similar among the four analyzed isolates, as depicted in Supplementary Figures 2A,B , respectively.
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The reciprocal regulation of phosphofructokinase-I and fructose 1,6-biphosphatase clearly indicate increased gluconeogenesis and decreased glycolysis in the isolates of P. A shift to gluconeogenesis has been described as a metabolic hallmark of fungal cells exposed to two-carbon sources.
Studies of the response of C. Comparison of protein profiles related to glycolysis and gluconeogenesis in P. ANOVA was applied to compare expression values among isolates, applying a cut-off of 1. Expression data were obtained using the Multi Experiment Viewer software V. B Changes in expression levels in yeast cells incubated with acetate in the four analyzed isolates are represented in a heat map format. Mean values of experimental triplicates are shown for down-regulation green and up-regulation red of genes of isolates Pb 01, Pb 03, Pb , and Pb EPM83 in the presence of sodium acetate.
Black indicates that no significant difference was observed. Three enzymes involved in ethanol production were differentially expressed in the presence of acetate. Acetate may provide ethanol because of the increase in aldehyde dehydrogenase and alcohol dehydrogenase. A high level of enzymes involved in ethanol production was observed, particularly for Pb 01 and Pb EPM83, which presumably produces ethanol from pyruvate, acetate, and acetaldehyde, as depicted in Figures 2A,B.
Comparative proteomic studies among isolates Pb 01 , Pb 2 Pb , and Pb EPM83 in nutrient-rich media revealed a high level of ethanol production in Pb 01 compared to in the other isolates, suggesting differential production of ethanol among isolates Pigosso et al.
Ethanol production has been related to fungi virulence.
The influence of alcohol dehydrogenase in fungal pathogenesis was observed in invasive pulmonary aspergillosis with an increase in the inflammatory response in the lung of mice infected with an alcohol dehydrogenase null mutant strain, and reduction in fungal burden Grahl et al. Ethanol measurement in P. A total of 10 6 cells was used for each sample, and the ethanol compound was quantified using an enzymatic detection kit UV-test for ethanol, RBiopharm, Darmstadt, Germany. Only Pb 03 showed up-regulated glucan 1,3-beta-glucosidase, which catalyzes successive hydrolysis of the beta-D-glucose units from the non-reducing ends of -beta-D-glucans, releasing beta glucose.
Aniline blue, which selectively stains 1,3-beta-D-glucan, was employed to estimate the amount of this polymer in the cell wall, as depicted in Supplementary Figure 3. As depicted in Supplementary Figure 3A , fluorescence was visibly reduced in Pb 03 grown with acetate. This enzyme catalyzes the formation of glucosamine 6-phosphate and is the first and rate-limiting enzyme in the hexosamine biosynthetic pathway controlling the flux of glucose into the hexosamine pathway.
The final product of the hexosamine pathway, UDP-N-acetyl-glucosamine, is an active precursor of numerous macromolecules containing amino sugars, including chitin in fungi and arthropods Badet et al. These enzymes participate in amino sugar metabolism and cell wall biosynthesis. Phosphoacetylglucosamine mutase reversibly converts N -acetyl-alpha-D-glucosaminephosphate to N -acetyl-D-glucosaminephosphate.
The products from this reaction are substrates to the enzymes glucosaminephosphate-deaminase and UDP- N -acetylglucosamine pyrophosphorylase, respectively. The first converts glucosaminephosphate and H 2 O to NH 3 and fructosephosphate, which is used in glycolysis and gluconeogenesis; the second converts N -acetyl-alpha-D-glucosaminephosphate to UDP- N -acetyl-D-glucosamine, which is used to produce chitin for the cell wall. These results suggest that Pb EPM83 can use polymeric carbohydrates precursors to obtain glucose by gluconeogenesis and synthesize chitin polymer into the cell wall.
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Comparison of protein profiles related to cell wall metabolism in P. A Representative diagram of the cell wall metabolism pathways depicting down-regulated green and up-regulated red proteins in the isolates, as cited above. The glyoxylate shunt, which is a shortcut for the decarboxylation steps of the TCA cycle, can allow the use of acetyl-CoA in the synthesis of cellular components Chung et al. Induction of transcripts encoding ICL and malate synthase was observed in phagocytized C. Thus, activation of this metabolic pathway enables the pathogen to survive and persist in the host in tissues with limited nutrients such as inside macrophages.
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Genes encoding the enzymes of the glyoxylate cycle, ICL and malate synthase, were induced in C. The role of the glyoxylate cycle in virulence has been described in organisms, such as Aspergillus fumigatus Olivas et al. Comparison of protein profiles related to TCA and glyoxylate cycle in P. A Representative diagram of the TCA cycle and glyoxylate cycle depicting down-regulated green and up-regulated red proteins in the isolates.
Regarding the genus Paracoccidioides , the induction of ICL was observed in Pb 01 during the transition from mycelium to yeast cells Bastos et al. The glyoxylate cycle was positively regulated in yeast cells of P. Increased expression of ICL was also observed in Pb 01 from 6 to 12 h under carbon starvation Lima et al. Acetyl-CoA can be consumed in the glyoxylate cycle for biosynthetic purposes or in the TCA cycle to generate cellular energy as reduced cofactors. Methyl citrate synthase is a key enzyme in the methyl citrate cycle and is essential for the degradation of propionyl-CoA in fungi and some bacteria, avoiding accumulation of propionyl, which is toxic Ibrahim-Granet et al.
The accumulation of propionyl in Aspergillus nidulans and A. Methyl citrate synthase is essential in A. Additionally, in Pb EPM83, the electron transport chain and ATP synthase complex were predominantly induced but no classes of proteins were repressed, as depicted in Supplementary Figure 4. Proteins of the different respiratory chain complexes were differentially regulated among isolates Supplementary Figure 4. Comparison of protein profiles related to amino acid catabolism in P.
B Representative diagram of the amino acid catabolism pathways depicting down-regulated green and up-regulated red proteins in the isolates, as cited above. The catabolism of amino acids is highly induced in Paracoccidioides.