The PL quantum yield also depended on heating time (Figure 2). Increasing the heating time led to increased PL quantum yield, and maxima occurred at 120 min. Such PL quantum yield increase could be ascribed to the improvement of the crystallization and annealing effect of defects. However,

further heating resulted in a decrease in PL quantum yield due to broad distribution and relatively small surface/volume ratio of the obtained QDs. Another evidence of the broad distribution is the increased full width at half maximum (FWHM) of the selleckchem resultant CdTe QDs, which broadened from 40 to 66 nm in the heating time of 0 to 270 min. With heating time longer than 300 min, there Stattic supplier were lots of black depositions in the solution, which may be caused by the oxidization and aggregation of CdTe QDs due to the destruction of MPA. Meanwhile, the see more PL quantum yield of the CdTe QDs decreases dramatically. Figure 2 Variation of quantum yield and FWHM of CdTe QDs at different reflux times. The as-prepared CdTe QDs were further characterized with XRD, TEM, HR-TEM, and XPS. As shown in Figure 3a, the diameter of the as-prepared CdTe QDs (refluxed for 120 min) is about 3 nm, which is very close to that estimated from Yu and colleagues’ empirical equation [21]. Typical HR-TEM image in Figure 3b indicated good crystalline structure of the CdTe QDs. The XRD pattern of CdTe QDs (Figure 3c) shows three diffraction peaks at 24.5°, 40.6°,

and 48°, which can be readily assigned to the (111), (220), and

(311) planes. Such characteristic diffraction pattern is the sign of the typical zinc-blend structure (JCPDS No. 65–1046). Figure 3 The as-prepared CdTe QDs. TEM (a) and HR-TEM (b) images, and XRD (c) pattern. Figure 4 shows the corresponding elemental composition by recording XPS core PIK-5 level spectra. Figure 4a shows an overview spectrum of the CdTe QDs. Different Cd and Te core levels can be seen. Furthermore, the main source of carbon, oxygen, and sulfur elements was from the stabilizer MPA. In our study, we focused on the Cd 3d, Te 3d, and S 2p levels. The Cd 4d and Te 4d levels have not been studied here because they are quite close to the valence band and, therefore, less reliable to analyze. The spectra of the Cd 3d and Te 3d level have been recorded in Figure 4b,c. The appearances of Cd 3d 3/2 peak at 411.9 eV, Cd 3d 5/2 peak at 405.2 eV, Te 3d 5/2 peak at 572.5 eV, and Te 3d 3/2 peak at 582.8 eV confirm the existence of cadmium and tellurium species in the CdTe QDs. This is in agreement with the previous reports [22] and further confirms the formation of CdTe QDs. Moreover, it can be seen clearly in the figure that two additional peaks appeared at binding energies of 576.0 and 586.6 eV, corresponding to the Te-O bonding states in CdTeO3, which are possible products from the oxidation reactions of CdTe QDs [23]. As mentioned in the experimental section, the CdTe QDs are capped with MPA.

The extracted proteins were subjected to immunoblotting analysis with anti-phospho-JNK, -phospho-p38 and -phospho-ERK1/2 antibodies. The BIBF 1120 datasheet stripped membranes were re-probed with anti-total-JNK, -p38, -ERK1/2 antibody to detect the total level of each MAPK protein present in the samples and to control for loading quantities. JNK and p38 were phosphorylated in cells co-incubated with the WT bacteria, in comparison to samples

obtained from untreated Caco-2 cells which showed no MAPK activation (Figure 1). Strong activation of JNK and p38 was observed at the 2 h time point, but not at earlier time points. In contrast, little or no phosphorylation of JNK and p38 was detected in cells incubated for 2 h with the heat-killed WT bacteria, indicating that the induction of activation of these two MAPK is an active learn more process of V. parahaemolyticus requiring viable bacteria. The patterns of ERK activation in response to V. parahaemolyticus were similar with lower phosphorylation signals detected. These studies indicate that V. parahaemolyticus induces activation of the

JNK, p38 and ERK MAPK signalling pathways via a mechanism requiring metabolically active bacteria. Figure 1 V. parahaemolyticus induces JNK, p38 and ERK phosphorylation in intestinal epithelial cells. Caco-2 cells were co-incubated with viable V. parahaemolyticus WT RIMD2210633 for 15, 60 or 120 min, with 50 μg/ml anisomycin for 30 min or with heat-killed ICG-001 supplier WT V. parahaemolyticus for 2 h. Cell lysates were prepared and proteins

separated by SDS-PAGE. Following transfer of proteins to nitrocellulose membranes, the membranes were probed with anti-phospho-JNK, -phospho-p38 and -phospho-ERK1/2 antibodies. The stripped membranes were re-probed with the corresponding anti-total-MAPK antibodies to control for equivalent protein loading. A. Representative image of MAPK immunoblot. Results are representative of at least three independent experiments. B. Quantification of MAPK activation. Results are expressed as the ratio of phospho-MAPK to total MAPK and as relative to levels in Caco-2 cells alone. Results indicate mean ± standard error of the mean (SEM) of three independent experiments. **P < 0.01; ***P < 0.001 vs medium. TTSS1 Selleck Etoposide of V. parahaemolyticus is responsible for activation of JNK, p38 and ERK in epithelial cells TTSS effectors of several pathogenic bacteria have been shown to modify MAPK activation levels in eukaryotic cells [24, 34–36]. As V. parahaemolyticus was able to induce phosphorylation of p38, JNK and ERK MAPK by an active process, we next investigated the involvement of the TTSS of V. parahaemolyticus in the activation of these MAPK. Bacteria lacking a functional TTSS1 or a functional TTSS2 were constructed by deleting the corresponding vscN gene for each secretion system.

Raw mass spectra acquisition The colonies were gently scraped with sterile plastic pliers to obtain an aliquot (approximately 3–4 mm in diameter) of fungal spores and

hyphae. This sample was first suspended in 75% ethanol HPLC. Next, the hydro-alcoholic solution was removed via 10 min centrifugation at 13,000 g, and the pellet was suspended in 10 NF-��B inhibitor μL of 70% formic acid (Sigma-Aldrich, France) by vigorously pipetting the sample up and down. After a 5-min incubation, 10 μL of acetonitrile HPLC (VWR International S.A.S., Fontenay-sous-Bois, France) was added, and the mixture was incubated at room temperature for 5 min. Finally, the sample was centrifuged for 2 min at 13,000 g. One microliter of the supernatant (consisting of a mixture of fungal proteins) was deposited for each reference strain subculture in 10 replicates on a polished steel target (MTP384, Bruker Daltonics GmbH, Bremen, Germany) and air-dried. Each MAPK inhibitor deposit was

then covered with 1 μL of a freshly prepared solution of α-cyano-4-hydroxycinnamic acid (HCCA) in 50% acetonitrile HPLC (VWR International S.A.S., Fontenay-sous-Bois, France) and 2.5% trifluoroacetic acid HPLC (TFA) matrix (Applied Biosystems®, Villebon sur yvette, France) [21]. The spectra were acquired after 650 shots in linear mode using an UltrafleXtreme™ instrument (Bruker Daltonics, Germany) in the ion-positive mode with a 337-nm nitrogen laser. The following adjustments were used: delay, 170 ns; ion source 1 voltage, 20 kV; ion source 2 voltage, 18.5 kV; mass range, 3–20 kDa; and measuring raster: spiral_small. An E. coli selleck kinase inhibitor calibration was performed before every experiment using a Bruker Bacterial Test Standard (Bruker Daltonics GmbH, Bremen, Germany). The data were automatically acquired using the AutoXecute function of the FlexControl v2.4 software and then exported into MALDI Biotyper v2.1 (Bruker Daltonics) software. Only the peaks with a signal/noise ratio ≥10 were considered. Constructing the reference mass spectra (RMS) The RMS were established

by combining i) 4 raw spectra obtained from one Neratinib solubility dmso subculture (RMS4); ii) 10 raw spectra obtained from one subculture (RMS10); iii) 20 raw spectra, 10 from two subcultures each (RMS20); or iv) 40 raw spectra, 10 from four subcultures each (RMS40) of a given reference strain using the “MSP creation” function of the MALDI Biotyper v2.1 software (Table 7). The following settings were applied (Bruker’s default parameters): Max. Mass Error of each single spectrum: 2000; Desired Mass Error of the MSP: 200; Desired Peak Frequency Minimum: 25%; and Max. Desired Peak Number of the MSP: 70. The modulation of the number of peaks and desired peak frequency minimum of the MSP creation parameters has been tested regarding the B1 library, and the modified parameters were tested on the B7 database (Table 4).

Nature 2009, 459:965–968.CrossRef 12. Hochbaum AI, Chen R, Delgado RD, Liang W, Garnett EC, Najarian M, Majumdar A, Yang P: Enhanced thermoelectric performance of rough GSK1210151A in vitro silicon nanowires. Nature 2008, 451:163–167.CrossRef 13. Yu JK, Mitrovic S, Tham D, Varghese J, Heath JR: Reduction of thermal conductivity in phononic nanomesh structures. Nature Nanotech 2010, 5:718–721.CrossRef 14. Tang J, Wang HT, Lee DH, Fardy M, Huo Z, Russell TP, Yang P: Holey silicon as an efficient thermoelectric material. Nano Lett 2010, 10:4279–4283.CrossRef 15. Fulkerson W, Moore JP, Williams RK, Graveb RS, McElroy

DL: Thermal conductivity, Selleck ACP-196 electrical resistivity, and Seebeck coefficient of silicon from 100 to 1300°K. Phys Rev 1968, 167:765–782.CrossRef 16. Serway RA: Principles of Physics. 2nd edition. Saunders College: Fort Worth; 1998. 17. Yu K, Li C, Wang R, Yang J: Production and properties of a spray formed 70% Si-Al alloy for electronic packaging applications. Mater Trans 2008, 49:685–687.CrossRef 18. Shim W, Ham

J, Lee K, Jeung WY, Johnson M, Lee W: On-film formation of Bi nanowires with extraordinary electron mobility. Nano Lett 2009, 9:18–22.CrossRef 19. Løvvik OM, Sagvolden E, Li YJ: Prediction of solute diffusivity in Al assisted by first-principles molecular dynamics. J Phys Condens Matter 2014, 26:025403.CrossRef 20. Savchenko IV, Stankus SV, Agadzhanov AS: Investigation of thermal conductivity and thermal diffusivity of liquid bismuth within the temperature range of 545–970 K. learn more High Temp 2013, 51:281–283.CrossRef 21. Xue W, Shi X, Hua M, Li Y: Preparation of anti-corrosion films by microarc oxidation on an Al–Si alloy. Appl Surf Sci 2007, 253:6118–6124.CrossRef 22. De Cicco MP, Turng LS, Li X, Perepezko JH: Nucleation catalysis in aluminum alloy A356 using nanoscale inoculants. Metall Mater Trans A 2011, 42A:2323–2330.CrossRef 23. Fang Sucrase W, Lo CY: On the thermal expansion coefficients of thin films. Sens Actuator A 2000, 84:310–314.CrossRef 24. Okada Y, Tokumaru Y: Precise determination of lattice parameter and thermal expansion coefficient of silicon between 300 and 1500 K. J Appl Phys 1984, 314:314–320.CrossRef 25. Jaccodine

RJ: Surface energy of germanium and silicon. J Electrochem Soc 1963, 110:524–527.CrossRef 26. Brandt R, Neuer G: Electrical resistivity and thermal conductivity of pure aluminum and aluminum alloys up to and above the melting temperature. Int J Thermophys 2007, 28:1429–1446.CrossRef Competing interests The author declares that he has no competing interests.”
“Background Malignant glioma is the most common primary brain tumor with grim prognosis. Current therapies, including surgery, radiation therapy, and chemotherapy, present limited efficacies for treating malignant glioma [1, 2]. Local control of the tumor is difficult in more than 80% of cases, because glioma cells infiltrate the surrounding tissues with high capabilities of migration and invasion.

The pellet samples after normalization to 12.5 O.D.600/ml, were boiled for 10 min in 1 x SDS-loading dye as above. After the run, proteins were either Coomassie stained or transferred

onto a polyvinylidene difluoride (PVDF) membrane (Immobilon P, Millipore) using a semi-dry blot. BvgS, a non-secreted protein control was detected using polyclonal mouse antiserum at a dilution of 1:1000 [21]. Pertactin (PRN), which is secreted by a non-T3SS dependent pathway, was identified using a monoclonal mouse antibody at a dilution of 1:1000 [22]. Bsp22, a T3SS substrate control, was detected using polyclonal mouse serum at a dilution of 1:10,000 [23]. Immunodetection was carried out by chemifluorescence using horseradish peroxidase-labeled goat anti-mouse IgG and the ECL plus® detection substrate (GE Healthcare). Chemifluorescent signals were visualized using a Typhoon scanner (GE Healthcare). selleck compound Genomic DNA extraction, PCR-based detection and genome sequencing DNA was extracted from overnight cultures of various isolates using the PureLink genomic DNA kit as per manufacturer’s instructions (Invitrogen Corporation, USA). PCR was performed according to the manufacturer’s instructions (0.5 U of iproof polymerase, 200 μM each of the four dNTPs and 1 μM each AG-881 solubility dmso primer) and supplemented with 3% dimethyl sulphoxide

(DMSO). Primers B77_QseC1F (5′- ATGACTTTGCAGCGCAGGTT −3′) and B77_QseC1R (5′- AGAAACGCGATCAGCACGGG −3′) or primers B77_QseC2F (5′- GGAGATCTTGCCGTCGCCAT-3′) and B77_QseC2R (5′-ACTTCCCATTGCGCGCGTAG-3′) were used to amplify qseC sequences, and primers B77_QseB1F (5′- GAGAATTCTTATTGTCGAAG-3′) and B77_QseB1R

(5′- GATTCCCAGTCATACAGCTT −3′) were used to amplify qseB. Cycling parameters were: one cycle of 98°C for 1 min; 25 cycles of 98°C for 10 s, 55°C for 20 s and 72°C for 30 s; and a final incubation at 72°C for 5 min. The PCR products were fractionated on 1% agarose gel using 1X TBE buffer containing 5 μg/ml ethidium bromide. PCR products of the extracted DNA were then purified Sclareol for sequencing using Qiagen’s QIAquick purification kit (Qiagen, Valencia, USA). Bordetella genomes were sequenced by the Sequencing Group at the Sanger Center and can be obtained from ftp://​ftp.​sanger.​ac.​uk/​pub/​pathogens/​bp. Construction of bscN and bteA in-frame deletion mutants To construct in-frame deletions of codons 171–261 in the bscN locus, allelic exchange was performed using pEGBR1005 suicide see more plasmid derivatives as previously described by Yuk et al. [15]. For construction of bteA in-frame deletions (codons 4–653), suicide plasmid pRE112-bteA was used as previously described by Panina et al. [11]. All mutants were verified by sequencing target open reading frames. Cell lines Cell lines used in this study were obtained from the American Tissue Culture Collection (ATCC).

Numerous chaperone-related genes respond to PAF26 and/or melittin, and the GO term “”response to unfolded protein stress”" was significantly repressed by melittin find more (Additional File 4.2). The co-chaperone regulator of chaperone activity STI1 was the

fifth most repressed gene by both peptides (Additional File 3.6). HSC82p and HSP82p are the two isoforms of the HSP90-like chaperone in yeast and are among the most abundant proteins in the cytosol [73]. HSC82 is considered to be constitutive while HSP82 is strongly induced by heat stress; the corresponding proteins are involved in folding of recalcitrant and denatured proteins. Contrary to HSP82, the HSC82 gene was strongly repressed by PAF26 and the deletion strain was more resistant to PAF26 killing (Figure 5C). Previous reports suggest that although nearly identical in sequence, these two

isoforms are not functionally equivalent [73]. Our study provides additional data on the involvement of protein chaperones and heat shock proteins in antimicrobial PCI-32765 clinical trial Peptide mode of action, which has been invoked in previous reports that include yeast and bacterial studies [9, 20, 21, 26]. Among the eleven chaperones repressed by melittin we found SSA2, coding for the CW protein that together with SSA1p was shown to bind the AMP Histatin 5 and promote peptide internalization [21]. In summary, AS1842856 chemical structure our findings help to confirm that permeation is not the unique effect of these and other AMP, and that additional (might be also overlapping) mechanisms that go beyond cell lysis are involved. The data presented support Benzatropine the

idea that CW reinforcement and modification are part of a general fungal response to peptides with different modes of action. However, a weakened CW is not necessarily indicative of a higher sensitivity to AMP. The importance of the response to unfolded protein stress or the sphingolipid biosynthesis, previously reported for other unrelated AMP, was also confirmed independently, therefore suggesting their broad contribution to activity of antimicrobial peptides. This study has also uncovered additional processes and genes that will be further analyzed in the near future, as is the case of the involvement of the metabolism of amino groups in the case of PAF26 or the YLR162W gene. Methods Synthesis of peptides PAF26 was purchased at >90% purity from Genscript Corporation (Piscataway, NJ, USA) and was acetylated at the N-terminus and amidated at the C-terminus. PAF26 was also synthesized labeled with fluorescein 5-isothiocyanate (FITC) by covalent modification of its N-terminus with FITC. Melittin was provided by Sigma-Aldrich (Cat nº M2272). Stock solutions of peptides were prepared in 10 mM 3-(N-morpholino)-propanesulfonic acid (MOPS) pH 7 buffer and stored at -20°C. Peptide concentrations were determined spectrophotometrically. Saccharomyces cerevisiae strains S.

The Curie temperatures of the LSMO nanolayers with and PLX-4720 purchase without In2O3 epitaxial buffering were 290 and 323K, respectively. A higher ferromagnetic ordering degree causes the LSMO films to have a higher saturation magnetization value and Curie temperature [16]. This reveals that more structural inhomogeneities in the LSMO nanolayer with In2O3

epitaxial buffering caused the double-exchange mechanism to have a greater depression degree [17]. Moreover, the higher moment in manganite thin films was attributed to a lower resistivity of the film [18]. This is in agreement with the CAFM measurements that convey that the LSMO nanolayer with In2O3 epitaxial buffering is slightly more resistant than the film without buffering. There www.selleckchem.com/products/cobimetinib-gdc-0973-rg7420.html is a large difference in the ZFC and FC curves’ low temperature range. ZFC curves display a broad summit peak. A larger difference in magnetization between the ZFC and FC curves in the low temperature region was observed for the LSMO nanolayer with In2O3 epitaxial buffering, which conveyed that randomly oriented magnetic domains are more difficult to align in the film. The subgrain boundaries among the LSMO nanograins, rough film surfaces, and interfaces caused an existence of disordered spins in the LSMO nanolayer. These disordered spins might play an important role in separating the magnetically ordered regions in the LSMO nanolayer [19]. This

caused the marked cluster glass state in the film. Figure 5c,d shows the magnetization-field (M-H) hysteresis curves at 50 K for LSMO nanolayers with and without In2O3 epitaxial buffering. selleck screening library The field was applied parallel to the

substrates. The respective in-plane saturated magnetization value was approximately 500 and 625 emu/cm3 for the LSMO nanolayers with and without In2O3 epitaxial buffering, respectively. The LSMO nanolayers with and without In2O3 epitaxial buffering have coercive fields that are 90 and 72 Oe, respectively. The crystal imperfections, such as surface roughness, subgrain boundary, and heterointerface, play important roles in determining the coercivity [7]. Several results conveyed that the surface roughness provides an extra hindrance to the magnetization reversal and induces an increase in coercivity accordingly Clostridium perfringens alpha toxin [20]. Moreover, a greater degree of structural inhomogeneities (rugged heterointerfaces and subgrain boundaries) in the LSMO nanolayer with In2O3 epitaxial buffering act as domain-wall pinning centers [17]. The relatively low coercivity is attributed to the high quality, low defect density of the LSMO nanolayer without buffering. The structural analyses support the observed M-H results. Figure 5 FC and ZFC M – T curves. Field-cooled and zero-field-cooled M-T curves of the LSMO nanolayer (a) with and (b) without In2O3 epitaxial buffering. M-H curve of the LSMO nanolayer (c) with and (d) without In2O3 epitaxial buffering.

A productivity study

by Dietz and Zeng [44] on the non-sterile fermentation of crude glycerol with the use of inocula received from three biogasworks demonstrated an increase in the synthesis of the main product even above the level of theoretical productivity. That was LY3023414 mw probably caused by the presence of strains able to metabolize glycerol other than C. butyricum and the introduction of an additional carbon source that was contained in the consortium. Analysis of some protein markers of environmental stresses The development of bioprocess technology has led to a greater production of metabolites, especially on an industrial scale. Large-scale production is connected with several problems such as the need to ensure optimal temperature and osmotic pressure as well as a non-inhibiting level of metabolites and to provide proper nutrients, and the fact that bacteria cells are prone to mechanical damage caused by shear force. In this study, in order to determine the C646 environmental stresses Thiazovivin solubility dmso resulting from the addition of glycerol in fed-batch fermentation some cell proteins considered to be stress markers were analyzed (Table 4). Table 4 Proteomic analysis of stress response in C. butyricum DSP1 Protein

names Gene/ORF names Number ID Mass (Da) q-value* Fold change** Fold change*** HSP20 CLP_1581 C4ILE7 17.07 0.0024 1.62 3.41 GroEL (HSP60) groL B1R088 57.90 0.0056 2.14 5.31 DnaK (HSP70) dnak C4IDG2 65.64 0.0165 1.32 3.72 HSP90 CLP_0987 C4IJL7 75.22 0.0076 0.23 0.31 SpoOA Spo0A B1QU80 31.45 0.0021 1.32 3.72 *q-value – statistical significance of obtained results. **fold change between samples from batch and fed-batch fermentation – after adding the first portion of glycerol (26th hour). ***fold change between samples from batch and fed-batch fermentation – after adding the second portion of glycerol (52nd hour). The differences between the level of the heat shock proteins HSP20, HSP60 (GroEL), HSP70 (DnaK), HSP90 and the transcription factors of sporulation process of SpoOA were observed. The literature points to Hsp60 (GroEL) as a protein associated with the response

of the genus Clostridium to osmotic, toxic and temperature stresses [58, 59]. Hennequin et al. [59] observed the influence of increased temperature (30-48°C) on the level of GroEL in C. difficile and found that after incubation at 43°C Adenosine triphosphate the level of this protein was 3 times greater than at 30°C. For C. acetobutylicum, a rise in the temperature from 30 to 42°C resulted in the appearance of 15 heat shock proteins belonging to the family HSP60 and HSP70 [60]. In the current work, heat shock proteins were detected in metabolically active cells able to synthesize 1,3-PD in batch and fed-batch fermentations. During batch fermentation the levels of all proteins studied were low whereas in fed-batch fermentation the amount of HSP60 increased twofold and of HSP20 1.5 times after adding the first portion of crude glycerol.

Only one double mutant in this gene showed a decreased resistance towards oxidative stress although it is annotated with 8 reactions

and functions. The S. Typhimurium dcoC gene encodes the gamma subunit of oxaloacetate decarboxylase. The check details protein also contains alpha and beta subunits, and it enables anaerobic growth on citrate and tartrate [50–52]. Despite its function in central metabolism, only one double mutant showed decreased survival under H2O2 stress. The ybeB gene product of S. Typhimurium has 97% homology to the E. coli ybeB gene product and homologues are widely distributed amongst bacteria and eukaryotes [53]. The E. coli ybeB has been shown to be associated with the large ribosomal subunit (50S) PU-H71 [54] and more recently, it was demonstrated to be important for survival during stationary phase as well as after transition from rich to poor medium [53]. It has been suggested that ybeB have a role in the down regulation of protein synthesis in stationary phase and under limited nutrition conditions by acting as a ribosomal silencing factor impairing the association of the 50S and 30S complexes. Therefore, the protein was denoted as RsfA (for ribosomal silencing factor) [53]. In our study strains with mutation in this gene were not ARN-509 mouse stably obtained, which may indicate that this gene

is essential. Apart from the decreased resistance to oxidative stress, some double mutants Amine dehydrogenase showed attenuated virulence in mice. The apparent interactions between these genes in virulence,

i.e. wraB with osmC and cbpA with dcoC is currently unknown, but the transcription of osmC has been shown to be upregulated 2–3 fold in murine macrophage-like J774-A.1 cells and cbpA to be downregulated 0.4 fold in both macrophages and HeLa cells during cell culture infections [55, 56]. As discussed above, mutation of a gene forming a hub in our networks would a priori according to network theory have be expected to result in broad-scale phenotypical changes of the population, however; we observed that hubs seem to have redundant functionality so that single hub deletion does not impact the phenotype and viability. This could be the result of evolution since mutations with a broad scale impact would be expected to be deleterious for the cell (Fisher 1930, cited in [57]. Becker et al.[18] analysed 700 enzymes of S. Typhimurium and identified 155 enzymes that were essential for virulence. Essential enzymes were exclusively associated with a very small group of pathways specialized in the biosynthesis of products that Salmonella cannot efficiently obtain from its host. This agrees with our results that genes involved in a high number of functions or adaptation to environmental conditions are not essential genes. In another study, more than 250 genes were reported to be essential for in vitro growth of Salmonella in LB-medium [58, 59].

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