FEMS Microbiol Lett 2005, 251:281–288.PubMedCrossRef

12. Korsak D, Popowska M, Markiewicz Z: Analysis of the murein of a Listeria monocytogenes EGD mutant lacking functional Z-IETD-FMK mw penicillin binding protein 5 (PBP5). Pol J Microbiol 2005, 54:339–342.PubMed 13. Zawadzka-Skomial J, Markiewicz Z, Nguyen-Distèche M, Devreese B, Frère JM, Terrak M: Characterization of the bifunctional glycosyltransferase/acyltransferase penicillin-binding protein 4 of Listeria monocytogenes . J Bacteriol 2006, 188:1875–1881.PubMedCrossRef 14. Glaser P, Frangeul L, Buchrieser C, Rusniok C, Amend A, Baquero F, Berche P, Bloecker H, Brandt P, Chakraborty T, Charbit A, Chetouani F, Couvé E, de Daruvar A, Dehoux P, Domann E, Domínguez-Bernal G, Duchaud E, Durant L, Dussurget O, Entian KD, Fsihi H, García-del Portillo F, Garrido P, Gautier L, Goebel W, Gómez-López N, Hain T, Hauf J, Jackson D, Jones LM, Kaerst U, Kreft J, Kuhn M, Kunst F, Kurapkat G, Madueno E, Maitournam A, Vicente JM, Ng E, Nedjari H, Nordsiek G, Novella S, de Pablos B, Pérez-Diaz JC, Purcell R, Remmel B, Rose M, Schlueter T, Simoes N, Tierrez A, Vázquez-Boland JA, Voss H, Wehland J, Cossart P: Comparative genomics of Listeria species. Science 2001, 294:849–852.PubMed 15. Guinane CM, Cotter PD, Ross PR, Hill C: Contribution of penicillin-binding protein homologs

to antibiotic resistance, cell morphology, and selleck inhibitor virulence of Listeria monocytogenes EGDe. Antimicrob Agents Chemother 2006, 50:2824–2828.PubMedCrossRef 16. Bierne H, Cossart P: Listeria monocytogenes surface proteins: from genome predictions to function. Microbiol Mol Biol Rev 2007, 71:377–397.PubMedCrossRef 17. Zhao G, Meier TI, Kahl SD, Gee KR, Blaszczak LC: BOCILLIN

FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins. Antimicrob Agents Chemother oxyclozanide 1999, 43:1124–1128.PubMed 18. Atrih A, Bacher G, Allmaier G, Williamson MP, Foster SJ: Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP5 in peptidoglycan maturation. J Bacteriol 1999, 181:3956–3966.PubMed 19. Sauvage E, Kerff F, Terrak M, Ayala JA, Charlier P: The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev 2008, 32:234–258.PubMedCrossRef 20. Zapun A, Contreras-Martel C, Vernet T: Penicillin-binding proteins and β-lactam resistance. FEMS Microbiol Rev 2008, 32:361–385.PubMedCrossRef 21. Gottschalk S, Bygebjerg-Hove I, Bonde M, Nielsen PK, Nguyen TH, Gravesen A, Birgitte Kallipolitis H: The two-component system CesRK controls the transcriptional induction of cell envelope-related genes in Listeria monocytogenes in response to cell wall-acting antibiotics. J Bacteriol 2008, 190:4772–4776.PubMedCrossRef 22. Severin A, Schuster C, Hakenbeck R, Tomasz A: Altered murein composition in a DD-carboxypeptidase mutant of Streptococcus pneumoniae . J Bacteriol 1992, 174:5152–5155.PubMed 23.

In contrast, more lactate was consumed in MR-1 than in the fur mutant (Figure 1C). This could be explained by the observation that there were more MR-1 cells after buy Panobinostat 36 hours’ incubation (data not shown), as the MR-1 grew faster than the fur mutant when lactate was provided as carbon source (Figure 2). To determine whether the ability of the fur mutant in metabolizing succinate and fumarate affects cell growth, we grew MR-1 and the fur mutant in M1 medium with 10 mM lactate plus succinate or fumarate.

Addition of succinate or fumarate significantly enhanced the growth of the fur mutant (Figure 2). Together, succinate and fumarate can indeed be similarly metabolized by MR-1 and the fur mutant of S. oneidensis and be used to support the cell growth when combined with lactate, though they are unable to support the cell growth as the sole carbon source. Figure 1 Comparison of MR-1 and the fur mutant for their ability to metabolize carbonate: (A) succinate, (B) fumarate and (C) lactate. 5 × 109 cells were incubated with 10 Kinase Inhibitor Library mM carbonate for 0, 36 and 54 hours. HPLC was used for carbonate measurements. Y-axis: the concentration of carbon source. Figure 2 The growth of wild-type (MR-1) and fur mutant in the presence of

10 mM lactate (lac) and (A) succinate (suc) or (B) fumarate (fum), which were supplied as carbon sources in defined medium. Cell density was measured at OD600 every thirty minutes for five days. Data 3-oxoacyl-(acyl-carrier-protein) reductase were averaged over triplicate samples. A recent microarray study comparing the gene expression profile of the fur mutant to that of MR-1 showed that neither the sdhCDAB operon nor the acnA gene was down-regulated [11], which was unlike the observations in E. coli. To confirm this, quantitative RT-PCR was carried out on acnA and sdhA, a gene of the SdhCDAB operon. The housekeeping gene RecA was used as the internal standard to normalize the gene expression levels. The levels of SdhA and AcnA relative to RecA in MR-1 are 0.14 and 0.06, respectively. Both genes exhibited little

change in expression in the fur mutant relative to MR-1 (Table 1). Therefore, the utilization of succinate or fumarate by the fur mutant (Figure 1) may be attributable to the persistent expression of TCA cycle genes. Notably, An putative iron uptake gene SO3032, which was expressed at the level of 0.04 relative to RecA in MR-1, was up-regulated in the S. oneidensis fur mutant. In contrast, the Fe-dependent superoxide dismutase encoded by sodB, a gene known to be regulated by Fur in E. coli [7], was repressed in the fur mutant (Table 1). This result agrees with previous observations that the transcript and protein expression levels of SodB are repressed in the fur mutant of S. oneidensis [10]. Table 1 Quantitative RT-PCR results.

References 1. EFSA: The Community Summary Report on see more Trends and Sources of Zoonoses, Zoonotic Agents

and food-borne outbreaks in the European Union in 2008. The EFSA journal 2010., 1496: 2. Smyth CJ, Smyth DS, Kennedy J, Twohig J, Bolton DJ: Staphylococcus aureus : from man or animal – an enterotoxin iceberg? In EU-RAIN, 3–4 December, 2004, Padua, Italy. Edited by: Maunsell B, Sheridan J, Bolton DJ. Teagasc – The National Food Centre; 2004:85–102. 3. Le Loir Y, Baron F, Gautier M: Staphylococcus aureus and food poisoning. Genet Mol Res 2003,2(1):63–76.PubMed 4. Thomas DY, Jarraud S, Lemercier B, Cozon G, Echasserieau K, Etienne J, Gougeon ML, Lina G, Vandenesch F: Staphylococcal enterotoxin-like toxins U2 and V, two new staphylococcal superantigens arising from recombination within the enterotoxin gene cluster. Infect Immun 2006,74(8):4724–4734.PubMedCrossRef 5. Ono HK, Omoe K, Imanishi

K, Iwakabe Y, Hu DL, Kato H, Saito N, Nakane A, Uchiyama T, Shinagawa K: Identification and characterization of two novel staphylococcal enterotoxins, types S and T. Infect Immun 2008,76(11):4999–5005.PubMedCrossRef 6. Bronner S, Monteil H, Prévost G: Regulation of virulence determinants in Staphylococcus aureus : complexity and applications. FEMS Microbiol Rev 2004,28(2):183–200.PubMedCrossRef 7. Cha JO, Lee JK, Jung YH, Yoo JI, Park YK, Kim BS, Lee YS: Molecular analysis of Staphylococcus aureus isolates associated with staphylococcal food poisoning in South Korea. J Appl Microbiol 2006,101(4):864–871.PubMedCrossRef 8. Kérouanton A, Hennekinne JA, Letertre C, Petit L, Chesneau O, Brisabois TGF-beta inhibitor A, De Buyser ML: Characterization

of Staphylococcus aureus strains associated with food poisoning outbreaks in France. Int J Food Microbiol 2007,115(3):369–375.PubMedCrossRef 9. Wieneke AA, Roberts D, Gilbert RJ: Staphylococcal food poisoning in the United Kingdom, 1969–90. Epidemiol Infect 1993,110(3):519–531.PubMedCrossRef 10. Casman EP: Staphylococcal food poisoning. Health Lab Sci 1967,4(4):199–206.PubMed 11. Payne DN, Wood JM: The incidence of enterotoxin production in strains of Staphylococcus aureus isolated from foods. Montelukast Sodium J Appl Bacteriol 1974,37(3):319–325.PubMed 12. Betley MJ, Mekalanos JJ: Staphylococcal enterotoxin A is encoded by phage. Science 1985,229(4709):185–187.PubMedCrossRef 13. Borst DW, Betley MJ: Phage-associated differences in staphylococcal enterotoxin A gene ( sea ) expression correlate with sea allele class. Infect Immun 1994,62(1):113–118.PubMed 14. Sumby P, Waldor MK: Transcription of the toxin genes present within the Staphylococcal phage phiSa3ms is intimately linked with the phage’s life cycle. J Bacteriol 2003,185(23):6841–6851.PubMedCrossRef 15. Smittle RB: Microbiological safety of mayonnaise, salad dressings, and sauces produced in the United States: a review. J Food Prot 2000,63(8):1144–1153.PubMed 16.

The results showed that the level of LATS1 expression was an independent prognostic factor for glioma (P<0.001) (Table 3). Figure 2 Reexpression of LATS1 in glioma U251 cells. A. Real-time PCR analysis indicated the highest mRNA expression of LATS1 in two cell clones pLATS1-2 and −4. B. Western blotting assay shows significantly increased protein expression of LATS1 in pLATS1-2 and −4 suppressed the expression of cell cycle factor CCNA1 protein compared to Control-vector

cells. β-actin was used as the internal control. Table 3 Summary of univariate and multivariate Cox regression analysis of overall survival duration Parameter Univariate analysis Multivariate analysis P HR 95%CI P HR 95%CI Age ≥55vs. <55 years 0.069 0.777 0.593-1.019       Gender Male vs. female 0.160 0.820 0.621-1.082       WHO grade Ivs.II vs.III vs.IV 0.000 1.715 1.454-2.023

0.000 1.463 1.233-1.735 KPS ≥80 vs. < 80 0.000 2.033 1.540-2.684 this website 0.000 2.437 1.810-3.283 LAST1 expression             Strong vs.Positive vs.Weak vs.Negative* 0.000 0.437 0.362-0.528 0.000 0.389 0.316-0.478 Overexpression of LATS1 in glioma U251 cells To study its biological functions, we introduced the LATS1 gene into the glioma U251 cell line using pCDF-GFP lentivirus expression vector. Five (5) stably transfected cell clones were obtained. Real-time PCR identified two cell clones (LATS1-2,-4) with the highest mRNA expression of LATS1 (Figure 2A). Further, LATS1 protein was highly expressed in two cell clones by western blotting assay with LATS1 antibody,while control clone cells lacked similar expression (Figure 2B). RAD001 research buy LATS1 inhibits cell proliferation in vitro To analyze the function of LATS1, we studied the rate of cell proliferation of LATS1-expressing LATS1-2 and −4 cells. The growth curves determined by MTT assay revealed that LATS1 significantly inhibited

cell proliferation of these two lines of cells compared to control clone cells (Figure 3A). In a colony formation assay LATS1-overexpressing LATS1-2 and −4 cells formed significantly less colonies than control clone cells (P < 0.001 ASK1 for both cell types) (Figure 3B, Table 4), suggesting the inhibitory effect of LATS1 on anchorage-dependent growth of glioma cells. Figure 3 Overexpression of LATS1 inhibted cell proliferation in vitro. A. The cell growth of Control-vector cells and pLATS1-2 and −4 cells, were examined by MTT assay over a seven-day period. *P < 0.05, as compared to control-vector cells. B. The cell growth of control-vector cells and pLATS1-2 and −4 cells, were examined by plate colony formation assay. *P < 0.05, as compared to control-vector cells. Table 4 Plate clone formation assay among pLATS1-2, pLATS1-4, and Ctr-vector cells Cells Number P value pLATS1-2 45.33 ± 4.16   pLATS1-4 34.67 ± 6.25   Ctr-vector 77.33 ± 7.12 p<0.

Group I represented the control and consisted of fish intraperitoneally (IP) injected with 0.7% NaCl. Group II was the experimental group, and the fish were IP injected with a dose of 2 mg/kg QDs (prepared in 0.7% MAPK Inhibitor Library research buy NaCl) per body weight. No food was supplied to the fish during the experimental period, and no obvious changes in fish body weight were recorded. After 1, 3, and 7 days from QDs injection, six fish from each group were sacrificed by trans-spinal dissection and the liver was quickly removed. Organs were immediately frozen

in liquid nitrogen and stored at -80°C until biochemical analyses were performed. Preparation of tissue homogenates and total protein measurements Liver was homogenized (1:10 w/v) using a Mixer Mill MM 301 homogenizer (Retsch, Haan, Germany) in ice-cold buffer (0.1 M Tris-HCl, 5 mM ethylenediaminetetraacetic see more acid (EDTA), pH 7.4), containing a few crystals of phenylmethylsulfonyl fluoride as protease inhibitor. The resulting homogenate was centrifuged at 8,000×g for 30 min, at 4°C. The supernatant was decanted, aliquoted, and stored at -80°C until needed. Protein concentration was determined using Lowry’s method with bovine serum albumin as standard [40] and was expressed as mg/mL. Oxidative stress markers Lipid peroxidation Lipid peroxidation was determined by measuring MDA content according to the fluorimetric method of Del Rio [41]. Briefly, 700 μL of 0.1 M HCl and

200 μL of a sample with a total protein concentration of 4 mg/mL were incubated for 20 min at room temperature. Then, 900 μL of 0.025 M thiobarbituric acid was added, and the mixture Etomidate was incubated for 65 min at 37°C. Finally, 400 μL of Tris-EDTA protein extraction buffer was added. The fluorescence of MDA was recorded using a Jasco

FP750 spectrofluorometer (Tokyo, Japan) with a 520/549 (excitation/emission) filter. MDA content was calculated based on a 1,1,3,3-tetramethoxy propane standard curve with concentrations up to 10 μM. The results were expressed as nanomoles of MDA per milligram of protein. Protein sulfhydryl groups assay The protein thiols were assayed using 4,4′-dithiodipyridine (DTDP) according to the method of Riener [42]. A volume of 100 μL of total protein extract was mixed with 100 μL of 20% trichloracetic acid (TCA) and thoroughly homogenized. After 10 min on ice, the samples were centrifuged at 10,000×g for 10 min. The pellet was rendered soluble in 20 μL 1 M NaOH and mixed with 730 μL 0.4 M Tris-HCl buffer (pH 9). Then, 20 μL of 4 mM DTDP were supplemented, and after 5-min incubation at room temperature (in the dark), the absorbance at 324 nm was measured. The concentration of PSH was quantified using a N-acetylcysteine standard curve with concentrations up to 80 μM. The values were expressed as nanomoles per milligram of protein. Carbonyl derivates of proteins CP were quantified using the reaction with 2,4-dinitrophenylhydrazine (DNPH) according to the method described by Levine [43].

Additional file 1: Tables S2 and S3 show the highly up-regulated and down-regulated genes in the PHA production phase to Selleck Talazoparib the growth phase (F26/F16), respectively. The highly down-regulated genes, i. e. genes with high induction in the growth phase, included flg cluster (H16_B0258-B0271) and two fli clusters (H16_B0561-B0567

and H16_B2360-B2373) related to flagella assembly, as well as several genes in che operon (H16_B0229-B0245) that are related to chemotaxis (Additional file 1: Table S3). Raberg et al. reported that flagellation was strongly occurred during growth and stagnated during PHA biosynthesis [25]. Similar results were obtained in a previous microarray-based comparison of R. eutropha H16 and a PHA-negative mutant PHB-4 [17]. A recent microarray analysis by Brigham et al. reported that PHB production was regulated by a stringent response,

because most of the upstream regions of the strongly up-regulated genes during nitrogen stress contained the consensus elements for σ54-family promoters [22]. Many of the genes were also highly up-regulated by 20–50 fold during the nitrogen-depleted PHA production phase in the present study, such as H16_A0359, H16_A2801, H16_B0780, H16_B0948, https://www.selleckchem.com/products/MDV3100.html and H16_B1156 (Additional file 1: Table S2). A gene cluster that encodes potential nitrogen-scavenging transporters and enzymes (H16_A1075-A1087) was also up-regulated in F26 by 4–16 fold to F16 (data not shown). The expression ratios were much less than 50-491-fold detected in the microarray analysis [22], but the present RNA-seq analysis supported the expression regulation for these genes by the stringent response. Transcriptome changes related to major metabolic processes and cellular functions Sugar degradation The genome analysis of R. eutropha H16 has identified three important clusters participated in fructose degradation in chromosome 2. The genes in cluster 1 (H16_B1497-B1503), which are frcRACBK, pgi2, and zwf2 were significantly induced in the growth phase (Figure 3), suggesting the important roles in transportation and conversion of extracellular fructose to 6-phosphogluconolactone for growth.

The genes in cluster 2, which are glk, zwf3, pgl, and edd2 (H16_B2564-B2567) have roles in sugar phosphorylation and Entner-Doudoroff (ED) pathway. The expression levels MTMR9 of these genes were low in F16 and F26, and slightly increased in F36. The cluster 3 (H16_B1211-B1213), which consists of a gene of putative 2-amino-2-deoxy-D-gluconate hydrolase and kdgK for glucosaminate degradation, and eda involved in ED pathway, was observed to be induced in the growth phase. Figure 3 Expression levels of genes involved in central metabolisms including PHA metabolism in R. eutropha H16 at growth phase F16, PHA production phase F26, and stationary phase F36 on fructose. The log2-transformed RPKM values are visualized using the rainbow color scale in the figure. Genes with the P value above the threshold (P > 0.05) are underlined.

A tentative overview of the global Brucella population structure was produced by comparison with published typing data. Results All strains could be typed at all loci, with few exceptions for panel 2B loci. At the loci bruce04, bruce09 and bruce16, multiple bands were observed in the PCR products of 12, 9 and 6 strains, respectively. This may suggest that in some occasions multiple alleles are present in the DNA preparation. Besides, two strains were negative in PCR either for bruce07 or bruce30. In 69 animals,

strains were initially isolated from different organs, PD0325901 contributing 121 extra strains. In sixteen among these animals, more than one genotype was observed (in one animal 5 different genotypes were found). In most cases, these genotypes were also observed in at least one other animal. In five cases, at least one of the genotypes was unique in the present collection, suggesting that the presence of multiple genotypes could be the result of a mutation event that occurred in the course of infection. Three of these new genotypes were the result of one repeat

unit changes at a single locus. The other two were a 2 repeat units change in bruce04 and a four repeat units change in bruce09. These observations suggest that occasionally the most highly mutable loci may vary in the course of https://www.selleckchem.com/products/LBH-589.html infection. They also do not exclude the possibility that animals carrying multiple variants may have been infected by multiple strains present within the community. The 294 investigated marine mammal Brucella isolates which originated from 173 animals and one patient clustered in 117 different genotypes using the complete MLVA-16 assay. One representative for each genotype and animal was used for analysis, totalling 196 strains (Figures 1, 2, 3). Three main groups were identified, the B. ceti group, the B. pinnipedialis group Progesterone and a third group comprising the human isolate from New Zealand. The 117 representative genotypes were compared with the 18 terrestrial

mammal Brucella reference strains and published data (Figure 4). The 3 clusters were clearly separated from all the terrestrial mammal isolates. Figure 1 MLVA-16 clustering analysis of 102 B. ceti strains defines three groups of strains. All B. ceti isolates cluster into a first part (genotypes 1 to 74) of the dendogram constructed from MLVA-16 testing of 294 Brucella strains obtained from 173 marine mammals (pinnipeds, otter and cetaceans) and one human patient from New Zealand. One strain per genotype and per animal is included (consequently some animals are represented by more than one strain), 196 entries are listed corresponding to 117 genotypes. In the columns, the following data are presented: DNA batch (key), genotype, strain identification, organ, year of isolation, host (AWSD: Atlantic White Sided Dolphin), host (Latin name), geographic origin, MLVA panel 1 genotype, sequence type when described by Groussaud et al. [25].

85% NaCl and plated; for SDS exposure, bacterial culture was treated with 0.1% SDS for Epacadostat 20 min; for sensitivity to hydrogen peroxide, bacterial culture was exposed

to 0.03% H2O2 for 20 min; for osmotic stress, bacterial culture was treated with 40% D-sorbitol for 40 min; for saline stress, bacterial culture was treated with 1.0 M NaCl for 20 min. Bacterial cells were serially diluted with NB medium and colony-forming units (cfu) were counted after being cultured on NA plates at 28°C for 48 h. Each test, plated in triplicate, was repeated three times with similar results. B Data shown are means and standard errors of three replicates from one representative experiment. Different letters in each data column indicate significant differences at P < 0.05 (Student's t-test). Mutation of gpsX has no impact on expression of virulence-related genes

Reduced virulence could result from down-regulation of key virulence genes. In order to test whether mutation of the gpsX gene affected the expression of virulence-related genes, quantitative reverse transcription-PCR Z-VAD-FMK price (QRT-PCR) assays were performed to monitor the expression profiles of six genes which were selected based on the alternated mutant phenotypes mentioned above. For total RNA preparation, the gpsX mutant and wild type strains were cultured to exponential phase in XVM2 medium that has been reported to mimic the environment of plant Thiamine-diphosphate kinase intercellular spaces [38]. The six target genes included one EPS biosynthesis gene (gumB), one LPS synthesis gene (rfbC), one catalase gene (katE), one TTSS component gene (hrcV), one TTSS regulator genes hrpX, and one TTSS effector gene (pthA). The results showed that none of the six genes was significantly differently expressed in the mutant 223 G4 (gpsX-) compared with wild-type strains when grown in XVM2 medium (Table 5), based on a student’s t-test (P < 0.05). Specifically, the primer set used for pthA is present

in pthA4 and its homologues pthA1, pthA2, and pthA3, but not in any other genes. Thus we refer it as pthA rather than differentiating them. The qRT-PCR result based on this primer should detect the expression of pthA4, pthA1, pthA2, and pthA3. It is very likely that pthA4, pthA1, pthA2, and pthA3 have similar gene expression pattern due to the same promoter sequences. The sequences are 100% identical in the 213 bp upstream of pthA4, pthA1, pthA2, and pthA3 including the predicated promoter region (data not shown). Consequently, the qRT-PCR result will represent the relative fold change in gene expression for pthA4, pthA1, pthA2, and/or pthA3 since it is relative fold change and not absolute expression value.

albicans (78) C. albicans (ATCC 90028) C. albicans (78) C. albicans (ATCC 90028) Gomesin 5.5 11 – - Fluconazole * 186 – - Gomesin + Fluconazole 0.6 + 3.5 1.3 + 14.3 0.11 0.19 * = not detected in up to 1.5 mM Evaluation of the antifungal activity of gomesin in mice with disseminated and Sirolimus clinical trial vaginal candidiasis Treatment with 5 mg/kg and 15 mg/kg of gomesin in mice with disseminated candidiasis effectively reduced the fungal burden of the kidneys, spleen and liver when compared with the control group (PBS-treated mice) (Figure 1A-C). Treatment with 10 mg/kg and 20 mg/kg of fluconazole also effectively controlled the infection (Figure 1A-C). Moreover,

treatment of vaginal candidiasis with

0.2% and 0.5% gomesin and 2% miconazole showed a significant decrease in colony forming units (CFUs) when compared with vehicle treatment (control group) (Figure 1D). The combination of gomesin and fluconazole or miconazole did not result in a synergistic effect. Figure 1 Gomesin treatment of mice infected with C. albicans. Evaluation of the number of colony forming units (CFU) per gram of tissue of the kidneys (A), spleen (B), liver (C) and vagina (D). The disseminated candidiasis was performed check details by intravenous injection of 3 × 105 yeasts suspended in 100 μL of PBS and vaginal candidiasis was performed by inoculating 3 × 106 yeasts suspended in 20 μL of PBS. The treatment was done one, three and six days after infection with C. albicans (strain 78). Animals were treated with different doses of gomesin (GOM), fluconazole (FLUCO) and miconazole (MICO). As Chlormezanone a control, infected animals received only PBS or cream (CREAM). * Indicates statistical significance (ANOVA with post-Tukey test, P < 0.05). Cytokine levels in kidneys of gomesin-treated mice Treatment with gomesin and fluconazole significantly increased the concentration of TNF-α, IFN-γ and IL-6 in the kidneys compared

to controls that were not infected and not treated as well as controls that were infected and treated with PBS (Figure 2). Figure 2 Cytokine levels in kidneys. Cytokine levels were evaluated in the kidneys of mice treated with gomesin (5 mg/kg) and fluconazole (20 mg/kg). Non-infected and untreated animals (NINF), as well as infected animals that received PBS, were used as controls. * Indicates statistical significance (t-test, P < 0.05) compared to the control INF. Evaluation of the effect of antifungal drugs in immunosuppressed mice with disseminated candidiasis The group of infected animals that received PBS (control) reached 100% mortality on the fifteenth day after infection. No statistically significant difference was observed between the group treated with gomesin (5 mg/kg) and the group treated with fluconazole (20 mg/kg), although there was an increase in survival during the last treatment.

LEO thanks the Brazilian agencies CNPq and FAPESP (Proc. 2012/51691-0) for

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