000, p = 0 000, and p = 0 008 respectively)

000, p = 0.000, and p = 0.008 respectively). Selleck Palbociclib Testosterone levels across time for both supplement groups were significantly

higher at 5POST and 15POST compared to PRE (p = 0.034 and p = 0.002 respectively), and significantly lower at 60POST compared to 5POST and 15POST (p = 0.017 and p = 0.013 respectively). Table 2 This table shows serum levels of total testosterone (ng/mL) and cortisol (μg/dL). Endocrine Response   PRE 5POST 15POST 25POST 40POST 60POST CORTISOL             PL 17.2 ± 5.1 24.8 ± 9.4 25.4 ± 9.7 22.9 ± 9.5 19.7 ± 9.8 17.1 ± 8.2 PS 17.5 ± 7.1 28.8 ± 11.3 25.9 ± 11 24.2 ± 10.5 20.9 ± 10.7 19.5 ± 11.2 TESTOSTERONE             PL 8.3 ± 2.9 11.3 ± 5.7 10.6 ± 3.5 9.7 ± 3.2 9.0 ± 2.1 8.6 ± 2.2 PS 8.9 ± 2.0 10.9 ± 3.6 10.8 ± 2.3 9.9 ± 1.7 9.9 ± 2.9 8.7 ± 3.2 Values are expressed as means ± standard deviation. There were no significant differences between supplement groups for serum total testosterone or cortisol (p > 0.05) Discussion The results of this study have shown that supplementation with PS daily

for 14 days significantly improved cognitive function prior to an acute bout of intense, lower-body resistance training. Supplementation with PS had no effect on mood, serum cortisol, or serum total testosterone. There were also no negative side-effects reported by any of the study participants in regards to PS supplementation. Previous research has shown evidence that cognitive function may be improved by supplementing with PS. Baumeister et al., concluded that 42 days of supplementation with 200 mg of PS resulted in changes in electroencephalogram (EEG) activity indicating a more relaxed state following induced stress. This particular study also examined Volasertib mouse cognitive function using the Stroop colour-word interference test and the D2 concentration test. Despite the fact that the participants in this study had improved EEG readings, there was no evidence of significant differences in the measures of cognitive function as observed Rutecarpine in our study [6]. According to a review article investigating the findings of PS supplementation in humans, Jäger et al., reported that significant improvements in cognitive

function have been observed in elderly populations, but not in younger populations [1]. Additionally, an experiment by Jäger and colleagues found that golfers had improved golf performance following 42 days of supplementation with 200 mg of PS and 15 g of carbohydrates [5]. This improvement in performance may potentially be related to the relaxation effect observed in the study by Baumeister. It is possible that a relaxed mind may be able to better focus on sports tasks that require a great deal of concentration on sport skill performance, thus resulting in improved performance. According to our research, it seems that the most beneficial effect of PS supplementation is improvement in cognitive function prior to exercise that could potentially translate into improved performance in sports requiring a relaxed state of mind.

The first and second scenarios, however, appear rather unlikely,

The first and second scenarios, however, appear rather unlikely, because hardly any macrophages

or monocytes were observed in histopathologic analyses at day one after infection. The third scenario appears quite likely, because histopathological analysis revealed a strong infiltration of neutrophils encasing ungerminated conidia. In contrast, functionally attenuated neutrophils and macrophages in corticosteroid-treated mice allowed development of invasive disease despite robust cellular recruitment in the lung parenchyma.   The treatment of mice with cortisone acetate or the combination of clodrolip and cortisone acetate led to 100% mortality and invasive fungal growth within the lung tissue. Although systemic administration of corticosteroids increases the number of circulating neutrophils by three- to fivefold [31], their ability to damage A. fumigatus hyphae is strongly reduced [32]. One day post-infection,

the lung tissue showed this website INCB024360 solubility dmso an extensive neutrophilic infiltration that surrounded germinating conidia. These neutrophils were able to delay uncontrolled tissue invasion by killing some proportion of fungal hyphae. As a consequence of the neutrophil infiltration severe tissue damage accompanied by parenchymal destruction (necrosis) was observed, leading to a decreased bioluminescence as described above. It is also noteworthy that under cortisone acetate treatment the efficiency of alveolar macrophages in inhibiting conidial germination after phagocytosis was strongly defective. None of the other treatment groups yielded hyphal germlings as early as one day post-infection. It could be assumed that this rapid germination is due to growth stimulation

via A. fumigatus corticosteroid receptors [33]. However, experiments, in which different concentrations of cortisone acetate were added to A. fumigatus cultures, neither stimulated conidia germination, nor increased the light emission (data not shown). Since clonidine cortisone acetate itself constitutes an “”inactive”" corticosteroid derivative, which is converted into “”active”" cortisol during metabolism in the liver [34], it might be possible that a stimulation of germination is only mediated by this metabolite rather than by cortisone acetate. Another possibility for the rapid germination of conidia is given by a neutrophil mediated tissue destruction releasing large amounts of nutrients from tissue cells, which enhanced the germination speed under this immunosuppresive regimen. The mild inflammation under RB6-8C5 treatment one day post infection and the absence of inflammation under cyclophosphamide treatment may not provide the same nutritional conditions leading to a delayed germination when compared to the cortisone acetate treatment. Another piece of evidence that supports the dependence on the number and functional integrity of neutrophils in the clearance of A. fumigatus is the observation that RB6-8C5 treatment renders mice highly susceptible to IA.

Therefore this gene including its putative native promoter region

Therefore this gene including its putative native promoter region was cloned onto a low copy expression vector and the resulting construct was transformed into BF4 mutant. Serum sensitivity tests were performed using the C. sakazakii ES5 wt strain, the BF4 (ΔESA_04103) mutant, the BF4 (ΔESA_04103) mutant containing an empty pCCR9 vector (BF4_pCCR9) and the complemented mutant BF4_pCCR9::ESA_04103.

The results of these experiments are depicted in Figure 2. An inactivation around 5 log during incubation in 50% human serum for 120 min was observed in the BF4 (ΔESA_04103) mutant as well as the mutant containing the low copy vector pCCR9, whereas the survival of the mutant MEK inhibitor with supplied vector pCCR9 and ESA_04103 was restored to 4 log reduction cfu ml-1 compared to T0 compared to the wt with 1.2 log reduction. We could, however, not completely restore the serum survival to wild type levels

in the complemented mutant. This Selleck BIBW2992 may be explained (in part) by the unknown copy number of the mRNA for this gene in the wild type during incubation in serum and/or by possible polar effects. Figure 2 Serum sensitivity test on C. sakazakii ES5 wt, mutant BF4 (ΔESA_04103), mutant containing the empty vector (BF4_pCCR9) and mutant complemented with the intact ESA_04103 gene (BF4_pCCR9::ESA_04103) after incubation in 50% HPS for 120 min (T 120 ). The means and standard deviations (±1SD) from two independent experiments are presented. An asterisk above the bars indicate statistically significant differences. Mutant 69_F1 was identified to be affected in a gene coding for a DnaJ domain family

protein. Members of this family are essential for their interaction with DnaK chaperone and activation of its ATPase Benzatropine activity. In Edwardsiella tarda it was recently demonstrated that DnaJ and DnaK play a crucial role in general bacterial virulence, in blood dissemination capacity [16]. Interestingly, by using the Tn5 approach we found an equally high number of knock out mutants, that showed an enhanced survival in human serum compared to the wild type. One of the obvious possibilities to explain this phenomenon would be the knock out of regulatory elements (repressors) which would lead to a subsequent activation/constitutive expression of the respective phenotype. Mutant 24_H4 (ΔrraA) may fall into this category. The region affected by the transposon in this mutant shows homology to the ribonuclease regulator protein RraA. This protein acts as an inhibitor of the essential endoribonuclease RNase E, which itself plays a crucial role in global mRNA metabolism as well as in the maturation of functional RNAs such as rRNAs, tRNAs, tmRNA, and small regulatory RNAs [17–20]. However, Lee et al.

All 4 heat shock proteins (HtpG, DnaK, GroEL and PA4352) were ele

All 4 heat shock proteins (HtpG, DnaK, GroEL and PA4352) were elevated in AES-1R compared to both PAO1 and PA14. Five proteins involved in oxidative stress resistance (PA3529, AhpC, PA4880, PA2331 and KatA) were altered in AES-1R, Selleck PF-2341066 with all except KatA present at increased abundance. Additional smaller functional clusters included the 3 enzymes of the arginine deiminase

pathway (ArcABC) and the ATP synthase alpha and beta subunits. We identified 2 proteins that were expressed from genes only encoded in the AES-1R genome (spots 26 and 43), and a further protein that was not contained within the PAO1 genome (spot 37). Previously hypothetical protein AES_7139 (spots 43 a-e; Figure 1) was the most abundant protein identified on the 2-DE gels of AES-1R and is present in multiple mass and pI variants. Variants exist at two masses, approximately 28 kDa and 16 kDa, with three pI variants at the higher mass (pI 5.2, 5.6, and

6.0), and two pI variants at the lower mass (pI 5.2 and 6.0). We subjected these spots to both MALDI-TOF MS peptide mass mapping and to LC-MS/MS for sequence characterization. We identified 9 peptide sequences that generated 90.8% sequence coverage for the RO4929097 ic50 predicted AES-1R gene (Figure 2). All variants generated near identical MALDI-MS spectra, suggesting the unusual migratory pattern on 2-DE gels are due to folding artifacts or poorly reduced ZD1839 order disulfide bonds [31–33]. The AES_7139 translated gene sequence is predicted to encode a protein of 16.7 kDa and with a pI of 5.3, suggesting the higher mass variants may be homodimers or artifacts of the gel process. The sequence contains a single cysteine residue through which a disulfide could be formed, however under the reducing conditions used to conduct 2-DE, it is more likely that a gel artifact results in the spot pattern. One of the peptides sequenced by MS/MS displayed a non-tryptic N-terminus 8-GTYLFQYAQDKDYVLGVSDEQSGAK-32 (2782.4093

m/z) cleaved between Met-7 and Gly-8 that suggests either N-terminal processing, or that Met-7 is the true N-terminus. We subjected the AES_7139 protein sequence to BLAST search and showed that there is 100% amino acid sequence identity with a hypothetical protein (PA2G_05851) from P. aeruginosa PA2192 (Blastp score 311, query coverage 100%, e-value 2e-83), an isolate from a chronically infected CF patient in Boston. Other matches displayed similarity to ricin B-type lectins, suggesting the protein might be involved in carbohydrate binding. Importantly, however, no other P. aeruginosa genomes within the Swiss-Prot database contained AES_7139 homologs. Figure 2 Predicted protein sequence of a P. aeruginosa AES-1R hypothetical protein ((A); AES_7139; spot 43a-e) characterized by MALDI-MS and LC-MS/MS (B).

However, flocculation in response to FeSO4 was less pronounced at

However, flocculation in response to FeSO4 was less pronounced at that iron concentration compared to 30 μM FeCl3 as quantified by measuring sedimentation rates (Figure 1B) as previously described [33]. Figure 1 Iron induced concentration dependent flocculation of C. albicans cells. (A) Microscopic beta-catenin inhibitor analysis. C. albicans SC5314 (WT) was incubated with different FeCl3 concentrations (indicated at the top left hand of each sub panel) or with 30 μM FeSO4 in RPMI at 30°C for 2 h. (B) Relative sedimentation rates of WT cells. Flocculation of cells was triggered

by 30 μM FeCl3 or 30 μM FeSO4 in RPMI and sedimentation rates were determined after incubation at 30°C for 2 h. Means and standard deviations of three independent samples are shown (n = 3). ** denotes P < 0.01 (student’s t-test). (C) Relative sedimentation rates of WT cells pre-cultured in the sufficient iron (YPD) or restricted iron medium (RIM) at 30°C for 3 h. Flocculation of cells was triggered by 30 μM FeCl3 in RPMI and sedimentation rates were determined after incubation at 30°C for 2 h.

Means and standard deviations of three independent samples are shown (n = 3). *** denotes P < 0.001 (student’s t-test). (D) Microscopic analysis of cycloheximide (CHX) or MeOH pre-treated cells. C. albicans SC5314 was pre-treated either with 500 μg ml-1 CHX or MeOH in RPMI at 30°C for 15 min. Iron or water were subsequently added and cells RAD001 price were incubated at 30°C for 2 h. Flocculation was also induced in yeast nitrogen base (YNB) medium containing 30 μM FeCl3 compared to 1.2 μM basal Fe3+ concentration (information given by the manufacturer), thus showing that the induction of flocculation was independent from the medium used (see Additional file 1). Cells may possess internal iron stores from pre-cultivation in an iron sufficient medium. Thus, ASK1 we investigated whether the iron content of the medium used during pre-cultivations influenced

the dependence of the flocculent phenotype on the iron concentration in RPMI. C. albicans was either pre-cultivated in a medium with sufficient iron, i.e. the rich yeast extract-peptone-dextrose (YPD) medium, or starved for iron by pre-cultivation in a medium with restricted iron availability (restricted iron medium: RIM). RIM resulted from addition of the iron chelator bathophenanthroline disulfonate (BPS) to YPD medium. As shown in Figure 1C, flocculation due to exposure to 30 μM Fe3+ was independent on the pre-cultivation medium: WT cells starved for iron by pre-cultivation in RIM flocculated upon exposure to 30 μM Fe3+ with a similar sedimentation rate as cells pre-cultivated in YPD. During all later experiments, we pre-cultivated C. albicans in YPD and added 30 μM FeCl3 as iron source to the respective medium of the working culture unless it is mentioned otherwise.

Chemotherapy 2003,49(1–2):33–35 PubMed

Chemotherapy 2003,49(1–2):33–35.PubMed Deforolimus in vivo 135. Marchetti F, Viale P: Current and future perspectives for levofloxacin in severe Pseudomonas aeruginosa infections. J Chemother 2003,15(4):315–322.PubMed 136. Neu HC: Aztreonam activity, pharmacology, and clinical uses. Am J Med 1990,23;88(3C):2S-6S. 137. Malangoni MA: Aztreonam in treatment of intra-abdominal infections. Urology 1988,31(6 Suppl):28–32.PubMed 138. Bradford PA: Tigecycline: A first in class glycylcycline. Clin Microbiol Newsl 2004, 26:163–168. 139. Townsend ML, Pound MW, Drew RH: Tigecycline in the treatment of complicated intra-abdominal and complicated skin and skin structure

infections. Ther Clin Risk Manag 2007,3(6):1059–1070.PubMed 140. Boucher HW, Wennersten CB, Eliopoulos GM: In vitro activities of the glycylcycline GAR-936 against 17-AAG gram-positive bacteria. Antimicrob Agents Chemother 2000, 44:2225–2229.PubMed 141. Papaparaskevas J, Tzouvelekis LS, Tsakris A, Pittaras TE, Legakis NJ, Hellenic Tigecycline Study Group: In vitro activity of tigecycline against 2423 clinical isolates and comparison of the available interpretation breakpoints. Diagn

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tigecycline: A worldwide perspective. J Antimicrob Chemother 2007, 60:449–450.PubMed 145. Scheetz MH, Qi C, Warren JR, Postelnick MJ, Zembower T, Obias A, Noskin GA: In vitro activities of various antimicrobials alone Flucloronide and in combination with tigecycline against carbapenem-intermediate or-resistant Acinetobacter baumannii. Antimicrob Agents Chemother 2007, 51:1621–1626.PubMed 146. Bartlett JG, Gerding DN: Clinical recognition and diagnosis of Clostridium difficile infection. Clin Infect Dis 2008,46(Suppl 1):S12–8.PubMed 147. Nobre V, Harbarth S, Graf JD, Rohner P, Pugin J: Use of procalcitonin to shorten antibiotic treatment duration in septic patients. A randomized trial. Am J Respir Crit Care Med 2008, 177:498–505.PubMed 148. Hochreiter M, Köhler T, Schweiger AM, Keck FS, Bein B, von Spiegel T, Schroeder S: Procalcitonin to guide duration of antibiotic therapy in intensive care patients: A randomized prospective controlled trial. Crit Care 2009,13(3):R83.PubMed 149.

aeruginosa PAO1 following 30% hepatectomy and drinking 25 mM [Pi]

aeruginosa PAO1 following 30% hepatectomy and drinking 25 mM [Pi], pH 7.5 ad libitum was significantly attenuated (from 60% to 30%) with an even further mortality see more attenuation down to ~ 10% when mice drank 25 mM [Pi], pH 6.0 (Figure 2A). Figure 2 Effect of pH on P. aeruginosa PAO1 virulence and pyoverdin production. (A) Survival in mice subjected to hepatectomy and intestinal injection of P. aeruginosa. All mice were drank either water (var. Hep+MPAO1), 25 mM potassium phosphate buffer at pH 6.0 (var. Hep+MPAO1+[Pi] pH 6.0), or 25 mM potassium phosphate buffer at pH 7.5 (var. Hep+MPAO1+[Pi] pH 7.5). Results were reproduced in 3 experiments, n = 16/group,

p < 0.05 in between pH7.5 and pH6.0 groups. (B) Survival in C. elegans feeding on P. aeruginosa PAO1 lawns. Results were reproduced in triplicate, n = 63/group, p < 0.05 in between pH7.5 and pH6.0 groups. (C) Pigmentation of P. aeruginosa PAO1 lawns grown at different phosphate and pH levels. The pH shift from 6.0 to 7.5 changes pigmentation on lawns containing Pi 25 mM. However, highly intense

pigmentation is observed in P. aeruginosa PAO1 when grown as lawns at low (<0.1 mM) phosphate independent of pH. (D) The enhanced production of pyoverdin under conditions of phosphate limitation is not affected by pH changes. In order to define the effect of pH on the lethality of P. aeruginosa, we used a more ordered host ZD1839 chemical structure model system of C. elegans where worms feed on P. aeruginosa lawns grown at varying levels of phosphate and pH. Briefly, nematodes fed on P. aeruginosa lawns grown on agarized Nematode Growth Media (NGM) in which 25 mM potassium-phosphate buffer was adjusted to pH 6.0 or pH 7.5. Suspension of P. aeruginosa PAO1 to create the bacterial lawns was also prepared in 25 mM [Pi] at pH6.0 or 7.5 respectively

to maintain consistency throughout the experimental period. As positive controls, parallel experiments were performed where worms fed on lawns of P. aeruginosa selleck kinase inhibitor grown on low phosphate medium (0.1 mM) similar to our previously published experiments [9]. Results demonstrated that the killing effect of P. aeruginosa against C. elegans at high phosphate concentration was enhanced at pH 7.5 compared to 6.0 (Figure 2B). Importantly, low phosphate conditions induced the highest lethality rate consistent with our previous findings and demonstrated that extracellular phosphate is a major cue that activates virulence [9]. Previous work from our laboratory demonstrated that red material accumulated in the digestive tube of dying of C. elegans worms feeding on P. aeruginosa at low phosphate that consisted of the P. aeruginosa virulence-related quinolone signal PQS complexed with iron (PQS-Fe 3+). This complex was determined to be toxic to C. elegans especially when combined with rhamnolipids [9]. In the current study, the red material was not observed when C. elegans fed on P. aeruginosa PAO1 lawns grown at [Pi] 25 mM, pH 7.5 suggesting a lack of either PQS or pyoverdin production.

The Membranes were stained with an enhanced chemiluminescence sol

The Membranes were stained with an enhanced chemiluminescence solution. Band intensities are normalized to β-actin as a loading control. Annexin see more V-FITC/PI staining and flow cytometry Cell cycle analysis: Cells were digested by typsin (0.25%) and fixed with cold 70% ethanol at 48 h after transfection. After washed

in phosphate-buffered saline, samples were incubated with 100 μl RNase A at 37°C for 30 min and stained with 400 μl propidium iodide (Sigma). Flow cytometric analysis was performed at 488 nm to determine the DNA contents. Apoptosis analysis: Cells were harvested as described above. After adding of 10 μl Binding reagent and 1.25 μl Annexin V-FITC, samples were suspended in 0.5 ml cold 1 × Binding Buffer and stained with 10 μl PI. The samples were then analyzed for apoptosis by flow cytometry. MTT assay Cellular proliferation was measured using MTT assay. 104 cells were seeded in 96-well plates and cultured with siRNA-DNMT1 at 37°C in a humid chamber with 5% CO2 for 24 h. 50 μl 1 × MTT was then added to each well and incubated with cells at 37°C for 4 h. After removal of supernatant, 150 μl DMSO were added to each well. The optical density (OD) was measured at 550 nm. The percentage of viability was calculated according to the following formula: viability% = T/C×100%, where T and C refer to the absorbance of Alpelisib price transfection group and cell control, respectively. MeDIP-qPCR assay Transfections were

performed as described above. MeDIP assay combined with qPCR were used to quantitatively assess the status of demethylation. Hela and Siha Cediranib (AZD2171) cells were transfected with siRNA and treated with 1.0 μM 5-az-dC (Sigma) respectively, and harvested at 72 h after incubation. Genomic DNA was extracted and randomly sheared to an average length of 0.2-1.0 kb by sonication. Dilution buffer and 60 μl Protein G Magnetic Bead suspension were added into the

fragmented DNA and allowed for more than 10 min of incubation. DNA was then incubated overnight at 4°C with 8 μg antibody (Epigentek) against 5-methylcytosine, followed by 2 h incubation with Mouse-IgG magnetic beads at 4°C. The methylated DNA/antibody complexes were then washed with 1 ml cold WB1, WB2 and WB3 buffer. Purified DNA was analyzed by qPCR on an Applied Biosystems 7500 Real-Time PCR System. Real-time PCR was performed in a total 8 μl volume containing 1 μl of DNA template, 5 μl of 2 × Master Mix, 1 μl ddH2O and 1 μl of each primer. The relative changes in the extent of promoter methylation were determined by measuring the amount of promoter in immunoprecipitated DNA after normalization to the input DNA: %(MeDNA-IP/Input) = 2^[(Ct(input)-Ct(MeDNA-IP)×100. Statistic analysis Statistical analyses were performed with SPSS version 13.0(SPSS, Chicago, USA). Quantitative results were given as mean ± SD and statistical analysis was carried out by t-test. P values less than 0.05 were considered as statistically significant.

Trees were rooted using as outgroups Aschershonia sp and/or Simp

Trees were rooted using as outgroups Aschershonia sp. and/or Simplicillium lamelicolla (both members of Hypocreales). Specifically, the phylogenetic tree produced from the ITS1-5.8S-ITS2 sequences obtained in this work and known related

sequences from the databanks, divided the majority of B. bassiana strains into two major clades (Clade A and C), with marginal support of each clade (Fig. 2). The only PXD101 cell line exception was three strains (namely U259, O46 and IR582) that grouped together, at the base of the remaining B. bassiana strains with significant bootstrap (99 and 84% for the NJ and MP analyses, respectively) and Posterior Probability support (99% for the BI analysis). Similarly, the three B. brongniartii strains, grouped with the respective sequences obtained from GeneBank and produced a sister clade to B. bassiana, whereas the B. vermiconia and B. amorpha strains were basal to B. bassiana and B. brongniartii (Fig. 2). They all clearly clustered to a group different from the other species of the order Hypocreales, with significant NJ (97%)

and MP (90%) bootstrap support. Based on 265 informative characters, 2,700 most parsimonious trees were constructed with tree length of 1,106 steps [Consistency Index (CI) = 0.56, Homoplasy Index (HI) = 0.44, Retention Index (RI) = 0.86, Rescaled Consistency Index (RC) = 0.48]. The relatively small number of informative characters may explain the

marginal MP bootstrap and PP support. SB203580 purchase The remaining previously known Beauveria species (B. geodes, B. nubicola, B. tundrense and B. parasiticum) grouped Morin Hydrate well with other Tolypocladium species as expected according to known taxonomic criteria [39, 40]. Figure 2 Phylogenetic trees constructed from unambiguously aligned ITS1-5.8S-ITS2 domain, as produced by NJ analysis. Clade credibility using NJ calculated from 1K replicates (upper numbers in roman), parsimony BS support calculated from 100 replicates (first lower numbers in italics) using PAUP and PPs produced by 2M generations (second lower numbers – in bold) using MrBayes, are shown. In the phylogenetics analysis of the ITS1-5.8S-ITS2 region, fungal species names and sequences obtained from GenBank are shown with their accession numbers in the figure. Fungal hosts are indicated as follows: in a circle, A, Araneida; C, Coleoptera; D, Diptera; H, Hemipetra; L, Lepidoptera; N, Nematoda; O, Orthoptera, T, Thysanoptera, R, Rotifera; ?, not known; in a square, H, Hymenoptera and no indication from soil or air. Geographic location is provided next to each isolate together with blue, orange, green, purple and magenta colour for the isolates originated from Europe, Asia, America, Africa and Oceania, respectively. B.

J Clin Microbiol 2002, 40:4004–4009 CrossRefPubMed 7 de CR, Soin

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