These data indicate that the hydrophobic surface properties of conidia are a prerequisite for appropriate surface sensing under nutrient-limiting conditions. In order to test the role of hydrophobins in conidial and hyphal hydrophobicity, and therefore possibly in hydrophobic surface sensing, we performed a systematic search for the presence of hydrophobin genes in the B. cinerea genome, analysed IWR-1 chemical structure their expression, and performed a functional analysis of three hydrophobin genes and a hydrophobin-like gene. Surprisingly, Milciclib cost mutants lacking all these genes were found to be phenotypically

indistinguishable from the wild type in all parameters tested. Our results challenge the concept that hydrophobins are generally required for the formation of hydrophobic surface layers in conidia and hyphae of higher fungi. Results Cloning and sequence analysis of Botrytis cinerea hydrophobin genes In the B. cinerea strain B05.10 genome sequence, three hydrophobin encoding genes were identified. Using Magnaporthe

oryzae class I hydrophobin Mpg1 [4] as a query in a blastp search, a protein (BC1G_15273) with weak homology was detected. Its size, arrangement of the eight conserved cysteines, and overall hydropathicity was similar to M. oryzae Mpg1 and other class I hydrophobins, and it was called Bhp1 (for ‘ B otrytis h ydro p hobin’). Using Liothyronine Sodium M. oryzae class II Oligomycin A solubility dmso hydrophobin Mhp1 [6] in another blastp query, the B. cinerea proteins BC1G_03994 (called Bhp2) and BC1G_01012 (called Bhp3) were found to show significant

homologies (E values < e-10). With blastp and tblastn searches using known hydrophobin proteins, no further hydrophobin genes were identified in the B. cinerea genome. The identification of hydrophobin encoding genes in fungal genomes is sometimes difficult due to their small size, the variable spacing between the cysteine encoding codons, and their low sequence homologies, in particular among class I hydrophobin genes. In order to identify further candidates for B. cinerea hydrophobins, a systematic search was performed in the published genome sequences of B. cinerea strains B05.10 and T4. The following search parameters were used: a) Total size of the protein smaller than 250 amino acids; b) Presence of at least 6 cysteines, four of them in a tandem arrangement separated by two further cysteine residues (full cysteine motive of hydrophobins: C-(Xn)-CC-(Xn)-C-(Xn)-C-(Xn)-CC-(Xn)-C); c) Prediction of a signal peptide. The search resulted in the identification of six further hydrophobin-like B. cinerea proteins, which all had a small size (98-234 aa), and a similar pattern of eight cysteines after manual correction of annotations (Table 1; additional file 1 : Table S1).

Further experiments will show to which extent this is due to reduced metabolic activity at this growth stage. It is also noteworthy, firstly, that proteins that are down-regulated in X. a. pv. citri biofilms are enriched for the GO terms ‘generation of precursor metabolites and energy’ and secondly, that the biofilm proteome mainly displayed changes in outer membrane and receptor or transport proteins suggesting that they may have a role in maintaining

a functional external structure as well as enabling Gefitinib Repotrectinib cost appropriate flow of molecules and signals required in this lifestyle. This study is the first report of a X. a. pv. citri biofilm proteome and the information gained will support future comparative analyses of differentially expressed genes and/or

proteins involved in biofilm formation. In addition, the data will also inform approaches to a more detailed physiological investigation into the function of individual proteins and their role in biofilm formation. Methods Bacterial strains, culture conditions and media X. axonopodis pv. citri was grown at 28°C in Silva Buddenhagen (SB) medium (5 g/l sucrose, 5 g/lyeast extract, 5 g/l peptone, and 1 g/l glutamic acid, pH 7.0) and XVM2 medium (20 mM NaCl, 10 mM (NH4)2SO4, 1mM CaCl2, 0.01 mM FeSO4, 5 mM MgSO4, 0.16 mM KH2PO4, Selleck AR-13324 0.32 mM K2HPO4, 10 mM fructose, 10 mM sucrose and 0.03% (w/v) casein acid hydrolysate (casaminoacid), pH 6.7). Bacteria were grown in SB with shaking until exponential growth phase and then diluted 1:10 in fresh XVM2 medium. For planktonic cultures 3-oxoacyl-(acyl-carrier-protein) reductase these dilutions were grown under agitation at 200 rpm on a rotating shaker and cells were recovered after 24 hours of growth at early stationary phase. For biofilms, 2 ml-aliquot of these dilutions were placed in 24-well PVC plates and incubated statically for seven days at 28°C. In both cases the population size was estimated by recovering bacteria by centrifugation and plating adequate dilutions on SB plates. After 48 hours colonies were counted and

related to the volume of the original cultures. The X. axonopodis pv. citri strain used in this work is named Xcc99-1330 and was kindly provided by Blanca I. Canteros (INTA Bella Vista, Argentina). Confocal analysis of biofilm architecture The GFP-expressing X. a. pv. citri strain previously constructed using the parental strain Xcc99-1330 [6] was used in the present study and statically grown in 24-well PVC plates, as described above, and biofilm development was analyzed at 1, 3 and 7 days by confocal laser scanning microscopy (Nikon Eclipse TE-2000-E2). Protein extraction and resolubilization for the proteomic analysis Cellular pellets of X. a. pv. citri planktonic and biofilm cultures were obtained by centrifugation and resuspended in urea buffer (9 M urea, 2 M thiourea and 4% (w/v) 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS)) with vigorous vortexing at room temperature.

Med Oncol 2011, in press. 30. Kim HR,

Lin HM, Biliran H, Raz A: Cell cycle arrest and inhibition of anoikis by galectin-3 in human breast epithelial cells. Cancer Res 1999,59(16):4148–4154.PubMed 31. Zhu X, Ohtsubo M, Bohmer RM, Roberts JM, Assojan RK: Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of selleck compound cyclin E-cdk2, and phosphorylation of the retinoblastoma protein. J Cell Biol 1996,133(2):391–403.PubMedCrossRef 32. Mac Kinnon AC, Kopatz J, Sethi T: The molecular and cellular biology of lung cancer: identifying novel therapeutic strategies. Br Med Bull 2010, 95:47–61.CrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions MK collected informations about patients (clinicopathological findings, survival time), carried out immunohistochemical studies, performed statistical analysis and drafted manuscript.

PP, AK and MG participated in collection of patient’s data. RJ coordinated the study and improved manuscript. All authors read and approved the final manuscript.”
“Background Reactive oxygen species (ROS) have been implicated as one of the causes of skeletal muscle fatigue during both aerobic and anaerobic exercise [1]. Although small increases in exercise induced ROS are important for stimulating cellular growth and maximising muscular force production [2, 3], excessive accumulation leads to a pro-oxidant environment which Pevonedistat nmr Nabilone can damage DNA, lipid and INCB018424 concentration protein membranes [4, 5]. Cellular damage may also impair cross-bridge cycling during skeletal muscle contraction and accelerate

the onset of fatigue [2, 6, 7]. This is supported by previous work suggesting that a bout of resistance training induces an excessive increase in ROS production which could be implicated in the reduction in skeletal muscle force generating capacity observed during exercise [4, 8, 9]. To maximise gains in muscular hypertrophy an RT session would typically involve exercising at a moderate intensity, defined as lifting a load between 65-85% of an individual’s one repetition maximum (RM), and using a high volume, typically 3–6 sets of 6–15 repetitions of the exercise [10]. Goldfarb and colleagues [8] found significant increases in the plasma ROS markers malondialdehyde (MDH) and protein carbonyls (PC) following arm flexor exercise involving four sets of a 12 repetition maximum (RM) load. Similar results have also been found for lower body resistance exercise where plasma measures of oxidised gluthanione (GSSG) and protein oxidation were elevated following 30 min of sub-maximal squatting exercise [4]. The primary cause of RT induced oxidative damage appears to result from increased xanthine and nicotinamide adenine dinucleotide phosphate (NADPH) oxidase production, together with ischemia–reperfusion which results in an increase in xanthine oxidase (XO) and peroxynitrite [9, 11, 12].

Two other proteins likely involved in cell morphology and peptidoglycan CHIR-99021 cost turnover were also decreased in abundance under in vivo conditions, the rod-shape determining membrane protein YfgA and the LysM domain protein YgaU. It remains to be demonstrated whether these changes represent a coordinated physiological response of SD1 cells to the hostile environment in the host gut, possibly promoting evasion from the immune system and lowering OM porosity for protection from any extracellular toxic substances released

by the host. S. dysenteriae type III secretion system and other virulence factors The virulence plasmid encodes the 30 kb spa-mxi type III secretion system (TTSS) and invasion plasmid antigens (Ipa proteins) required for invasion of host cells [53]. The TTSS is comprised of a membrane-spanning protein complex which includes ca. 50 proteins, including Mxi and Spa proteins involved in assembly and regulation of the TTSS, chaperones (IpgA, IpgC, IpgE and Spa15), transcription activators (VirF, VirB and MxiE), translocators (IpaB, IpaC and IpaD) and ca. 25 effectors [8, 54]. Invasion is followed by entry of Shigella into colonic epithelium cells via the basolateral

membrane. Further bacterial invasion and lateral spreading of the bacteria within the colonic epithelium is mediated by host cell actin OICR-9429 supplier polymerization. The surface protein IcsA encoded by the virulence plasmid is responsible Cell Penetrating Peptide for actin-based BIBF 1120 nmr motility required for intra- and inter-cellular spread of the bacteria [55]. Shigella manipulates the host innate and adaptive immune system via the Osp family of proteins [56]. In the present study, we identified many components of the TTSS, including 15 Mxi-Spa proteins and 16 effectors and their chaperones (Additional File 1, Table S1). The TTSS has been reported as being assembled with a few effectors and chaperones when cultured in vitro, and activated only after contact of bacteria with host cells [8]. Here, many TTSS proteins were identified in both the in vitro

and in vivo datasets, including membrane associated Mxi and Spa proteins, Ipa effectors and Spa chaperones. Spa15 is a chaperone for the Osp family of effectors (OspC1, OspC2, OspC3) and also for the IpaA and IpgB2 effectors; while IpgC is a chaperone for IpaB and IpaC [8]. Activation of TTSS results in the induction of the transcription of genes encoding a second set of effectors under the control of MxiE and IpgC, including several spa genes. The OspC2 and OspC3 effectors and the IpgA and Spa32 proteins were detected only under in vivo conditions. Activation of the TTSS is followed by formation of the TTSS translocator pore which requires the IpaB, IpaC and IpaD effectors [5, 57]. IpaB in particular induces apoptosis in host macrophages leading to inflammatory infection [58].

Animals and drug treatment Male or female Sprague–Dawley rats (180 to 230 g) were employed for the experiments (Shanghai Experimental Animal Center, Chinese Academy of Sciences). Five rats were kept in individual cages with water and food available ad libitum. The animal room

was maintained at 21°C to 23°C, with a 12-h light–dark cycle. All experimental procedures were approved by the Committee of Laboratory Animals, Chinese Academy of Sciences. Rats were intraperitoneally (i.p.) administered with 70-mg/kg dose of 1% PTZ (dissolved in saline) to induced auditory evoked potential (AEP). Control animals received the same amount of saline injections. The seizures were rated according to the following criteria [34, 35]: stage 0, no VX-770 in vitro response; stage I, ear and facial

twitching; stage II, myoclonic jerks without upright position; stage III, myoclonic jerks, upright position with bilateral forelimb clonus; stage IV, clonic-tonic seizure; and stage V, generalized clonic-tonic seizures, loss of postural control. Experimental rats were divided into four groups as follows: group 1, rats were treated with saline; group 2, rats were i.p. injected with a dose of 70 mg/kg PTZ to induce the onset of seizures; group 3, rats were i.p. co-administered with a dose of 70 mg/kg PTZ since i.p. injected with a dose of 500 mg/kg taurine after 30 min; and group 4, rats were i.p. co-administered with a dose of 70 mg/kg PTZ since i.p. injected with a dose of 500 mg/kg GABA after 30 min. After 1 h, the animals were killed, the brains were dissected, SRT2104 order the cerebral cortex and hippocampus tissues were removed, and blood was withdrawn. The brain tissue was rinsed in ice-cold normal saline, added to nine times ice-cold normal saline, homogenized, and centrifuged at 5,000×g for 15 min at 4°C. The blood nearly was centrifuged at 3,000×g for 15 min. The supernatant and serum were obtained and stored in a −20°C refrigerator for MDA Blasticidin S research buy assays and antioxidant enzymes’ (SOD, GSH-Px) activity assays. The

protein concentration was determined by Coomassie Brilliant Blue method. MDA assay and antioxidant enzyme activity measurement The MDA and antioxidant enzymes’ (SOD, GSH-Px) activity of the cerebral cortex and the hippocampus tissue and blood from PTZ-induced AEP were evaluated by MDA assay and antioxidant enzymes’ (SOD, GSH-Px) kits according to the manufacturer’s instructions. Statistics Data were shown as mean ± S.E.M. Statistical evaluation was carried out by one-way analysis of variance (ANOVA) followed by Scheffe’s multiple range tests. P < 0.05 was considered to be significant. Results Incubation products assayed by HPLC and fluorescence The mixture was separated at acidic pH through HPLC and fluorescence after amino acids (5.0 mM) were incubated with MDA (5.0 mM) in 0.2 M PBS, pH 7.4, at 37°C for 48 h.

Serial dilutions were plated on GC agar with and without spectinomycin (to a final concentration of 50 mg/l) and incubated overnight. The spectinomycin OFF to ON switching rate was determined by dividing the number of colonies on GC plates containing spectinomycin by the number check details of colonies on plain GC plates. Phase variation experiments were repeated at least 5 times for each strain. Significance in differences in phase variation frequency was calculated by the Kruskal-Wallis test. Results

and discussion Fpg is nearly ubiquitous among bacterial species and is highly conserved both within annotated neisserial genome sequences and clinical Mc isolates [10], as well as between evolutionarily distant prokaryotes. We examined the activity and specifiCity of recombinant Mc Fpg purified to homogeneity towards representative substrates resulting from oxidative DNA damage, 8oxoG and faPy, and detected prototype Fpg glycosylase activity. Previously, we have shown a synergistic effect between the two GO components MutY and Fpg in Mc [9]. Together, these findings emphasize a distinct role for Fpg in the defense against the deleterious effects

of reactive oxygen species. The putative Mc fpg open reading frame (ORF) consists of 828 bp SCH727965 mw and contains a DNA uptake sequence (DUS) (5′-GCCGTCTGAA-3′) (Figure 1A). The Mc genome harbours approximately 2000 copies of this highly conserved 10 bp sequence, which is required for efficient transformation [23]. A 12-mer DUS with two P505-15 order additional bp upstream of the core 10 bp repeat element improves the transformation efficiency [24]. The Mc fpg gene contains one 11-mer. A single

complete DUS or AT-DUS (10-, 11- or 12-mer) may promote the reacquisition of a gene by transformation if it is damaged or deleted and DUS occurs at higher densities in genome maintenance genes than in other house-keeping genes [25]. Figure 1 N. meningitidis (Mc) Fpg. (A) Physical map of the Mc fpg open reading frame and flanking regions. The fpg gene Sorafenib purchase contains a DNA uptake sequence (DUS). Primers KT1b and KT2b employed in cloning of the Mc fpg gene are depicted. The gene organization of the Mc fpg flanking regions is identical in all available neisserial genomes. NMB1296 encodes a hypothetical protein with sequence homology to DNA methyltransferases. A promoter is predicted upstream of NMB1296 (black arrow). The fpg and the lysophophatidic acid acyltransferase nlaA genes are putatively co-transcribed [27], although an inverted repeat (containing DUS) associated with transcription termination or attenutation is found downstream of the fpg gene. NMB1297 is COG-annotated mltD (membrane-bound lytic murein transglycosylase). NMB1293 is a hypothetical protein. The distribution of DUS and degenerate DUS is indicated. (B) Structural modeling of Mc Fpg based on E.

High-resolution transmission electron microscopy (HRTEM) micrographs of the samples buy CB-839 were taken using a JEOL 2010 HRTEM (JEOL Ltd., Tokyo, Japan). A PerkinElmer Lambda 750 UV/VIS/NIR spectrometer (PerkinElmer, Waltham, MA, USA) was employed to obtain the optical transmission, reflectance, and absorbance of the samples. The optical reflectance spectra were measured at an incident angle of 45° to the samples. Electrical properties of the samples were studied using a Keithley Source Measure Unit 236 (Keithley Instruments, Inc.,

Cleveland, OH, USA) for current-voltage (I-V) measurement. Prior to the I-V measurement, gold electrodes (in circular shape, Stattic diameter of about 2 mm) were evaporated on top of the sample using a thermal evaporator. The distance between two consecutive electrodes was fixed at 2 mm. Results and discussion Figure 1a shows the FESEM images of the In2O3 NPs formed by the evaporation of In wires in a N2O plasma environment. A high density of NPs with an average size of approximately 40 ± 9 nm was found to be randomly distributed on the quartz substrate. A magnified FESEM image (Figure 1b) reveals the appearance of the NPs. Structures with different numbered

facets (three, four, five, six, and eight faces) corresponding to triangular, rhombohedral, pentagonal, hexagonal, and octahedral shapes, respectively, can be recognized from the sample. These structures indicate that the In2O3 NPs formed are in crystalline state. The observed In and O signals from the energy-dispersive X-ray (EDX) spectrum (Figure 1c) confirm selleck compound the composition of the In2O3 NP. The Si signal that PIK-5 appeared in the EDX spectrum originated from the quartz substrate. The color of the In2O3 NPs changed from white to yellowish upon thermal radiation treatment (Additional file 1: Figure S2). The films appear to be more transparent after the treatment. The FESEM image depicted in Figure 1d reveals a compact nanostructured

film for the sample after undergoing thermal radiation treatment. The sizes of the nanostructures vary largely from 60 to 300 nm. Meanwhile, we observed that the nanostructures mainly consist of shapes with fewer facets which are triangular or rhombohedral (Figure 1e). The EDX spectrum taken from the nanostructured films (Figure 1f) showed high signals of In and O, reflecting high purity of the nanostructured In2O3 films formed by this technique. The signal of the substrate (Si) was largely suppressed due to the closely packed structure of the In2O3 film, which limited the emission of X-ray from the substrate atoms after the thermal radiation treatment. Figure 1 FESEM images and EDX spectra. FESEM images of (a, b) as-grown In2O3 NPs and (d, e) thermal radiation-treated In2O3 NPs. (c, f) EDX spectra of the as-grown In2O3 NPs and thermal radiation-treated In2O3 NPs, respectively.

The modified FAB medium was supplemented with glucose (100 mg l-1) as carbon source and isopropyl-thio-beta-galactoside (IPTG; 12 mg l-1) to ensure expression of fluorescent proteins from the PA1/04/03 promotor. The flow system was assembled and prepared as described previously TPCA-1 molecular weight [24]. A microscope cover slip of borosilicate (Knittel 24 × 50 mm st1; Knittel Gläser) was used as substratum. The flow chambers were inoculated by injecting approximately 2 × 106 cells, into each flow chamber

with a small syringe. After inoculation, the flow chambers were left find more without flow for 1 h, and medium flow (0.2 or 0.8 mm s-1 corresponding to laminar flow and Re numbers of 0.3 and 1.3,

respectively) was started using a Watson Marlow 205 S peristaltic pump and the system was incubated at 30°C. Microscopy and image acquisition Biofilm formation was monitored by CLSM four, 24, 48, and 72 hours after inoculation. Microscopic observations and image acquisitions were performed with a Zeiss LSM 510 CLSM (Carl Zeiss, Jena, Germany) using a 40 ×/1.3 oil objective. I-BET-762 mw The microscope was equipped with lasers, detectors and filter sets for detecting CFP and YFP fluorescence. Simulated three-dimensional images were generated using the IMARIS software package (Bitplane AG, Zürich, Switzerland). Quantification of biofilm formation and statistical analysis For quantitative analysis of the biofilms, CLSM images were analysed by the computer program Adenosine COMSTAT [25]. The total amount of biomass on the surface, the relative substratum coverage

and the average thickness of the biofilm were calculated. Differences between the wild type and each mutant in the three parameters were compared by using a two-tailed independent t-test. P values below 0.05 were considered to be statistically significant. Fimbrial switch orientation assay A modification of a previously described method was used to determine the orientation of the fim-switch in K. pneumoniae biofilms [18, 26]. Biofilm samples were obtained by aspiration of the biofilm from individual flow cell channels by use of a syringe. All inoculum and biofilm samples were boiled for 5 min in PBS immediately after collection and then kept at -20°C until use. After thawing, the samples were boiled for 5 min, centrifuged at 12,000 g for 15 min and 2 μl of the supernatant used as template for PCR. Primers CAS168 and CAS169 (Table 1) were used to amplify an 817 bp region containing the fim-switch by use of the Expand High Fidelity PCR System (Roche).

This induction of DON was confirmed in an in vivo experiment in which flowering wheat plants were infected with F. graminearum and subjected to a sub lethal

dose of prothioconazole + fluoxastrobin. Previous work on F. culmorum demonstrated no or a negative effect of several strobilurins and triazoles on DON production [24] so the observed phenomenon of an increased DON production by F. graminearum induced by sub lethal concentrations of triazole fungicides might be a strain- or species-specific phenomenon. It is tempting to speculate whether this accumulation of DON is the consequence of the preceding accumulation of H2O2 as such being the first link in a signalling cascade activated upon sub lethal triazole treatment. Although this key role Selleckchem ZIETDFMK of H2O2 is not unambiguously demonstrated in the present study, the amount of evidence is compelling: H2O2 precedes accumulation of DON, combined application of catalase (eliminating H2O2 from the medium) inhibited DON accumulation. In addition, the application led to a reduced activity of the triazole fungicide. Application of H2O2 to F. graminearum cultures led to a reduced germination

and prompt induction of DON biosynthesis 4 h after H2O2 application. This additional experiment proves that H2O2 accumulation is necessary and sufficient to initiate DON production. The activation of the DON biosynthesis machinery by H2O2 is in concordance with previous observations C59 wnt price by the group of Barreau [17, 19, 20] who demonstrated that exogenously applied H2O2 by

repeated single or pulse-feeding resulted in accumulation of DON. However, these authors only monitored increases in DON at late time points such as 10 to 30 days after H2O2 application whereas we AZD1480 molecular weight observe a clear prompt activation of DON production within hours. From a physiological point Cyclooxygenase (COX) of view the effect of H2O2 during the initial germination events is logic and in line with the physiology of an in field F. graminearum infection: H2O2 is one of the key regulators in the plant defense system upon pathogen attack [30]. Therefore, this molecule is encountered frequently and at early time points by the pathogen in the interaction with its host. Previous work by the group of John Manners demonstrated beautifully that DON itself can induce hypersensitive cell death and H2O2 during infection [5] and as such underpinning the interaction between both molecules. Astonishingly, very low concentrations of H2O2 promoted conidia germination rate where a reduction was expected. We hypothesize that during germination events, very small amounts of H2O2 are beneficial and necessary in the primordial germination- and hyphal extension events. It is known that H2O2 is necessary in de novo synthesis of cell wall and membrane components during germination and hyphal extension.

It can cause a variety of clinical manifestations from mild gastroenteritis to bacteremia and typhoid fever. The global burden of nontyphoidal Salmonella gastroenteritis has been estimated

selleck chemicals llc to be 93.8 million cases of gastroenteritis each year, with 155 000 deaths [1]. In Africa, non-typhoidal Salmonella has consistently been reported as a leading cause of bacteremia among immuno-compromised people, infants and newborns [2, 3]. However, the sources and transmission routes of Salmonella in developing countries are poorly understood due to the lack of coordinated national epidemiological surveillance systems [4, 5]. In general, the primary sources of salmonellosis are considered to be food-producing animals such as cattle, poultry and swine [6]. The pathogens are mainly disseminated by trade in animals and uncooked animal food products [7]. The process of removing the gastrointestinal tract during slaughtering of food animals is regarded as one of the most important sources of carcass and organ contamination with Salmonella at abattoirs [8]. Also asymptomatic pet animals are a potential source of infection, especially species with high fecal carriage rates of Salmonella[9]. African pygmy hedgehogs kept as pets have Palbociclib order previously been associated with cases of human salmonellosis

[10]. The development and the accumulation of resistance to antimicrobials in foodborne pathogens are a major problem for public health. Multi-resistant Salmonella may acquire their resistance genes from microbiota of production selleck compound animals before being transmitted to humans through

food chain [11, 12]. Due to the lacking surveillance programs in Burkina Faso, as in the most of Africa, information on the prevalence of Salmonella and other enteropathogens in food stuffs is limited. However, our previous study on the prevalence of enteric bacteria on retail meats sold at the markets in Ouagadougou, Burkina Faso, revealed that 37% of the chicken, 13% of the beef intestines, Baricitinib and 7% of the mutton samples were contaminated by Salmonella[13]. The most common serotypes detected were S. Derby and S. Tilene. In a following broader study on chicken carcasses in Burkina Faso, up to 57% of the carcasses were found to be contaminated by Salmonella, S. Derby again being the most common serotype [14]. In order to better understand the origin of the pathogens, in the current study, we sampled the feces of the common food animals during slaughter. Since previously S. Tilene has mainly been recovered from African pigmy hedgehogs kept as pets in North America or Europe [15, 16], we included hedgehogs, which are common on the grassy pastures in Burkina Faso and also consumed as food, in our study.