etli CFN42 is not unique to this strain. A screening of the location of panCB genes among members of the Rhizobiales, showed that the occurrence of these genes in plasmids is a highly conserved trait among R. etli and R. leguminosarum strains. Furthermore, the synteny of the panCB, oxyR, katG genes in R. etli CFN42 is conserved in R. etli CIAT652 and in R. leguminosarum strains 3841, WSM1325 and WSM2304. In contrast, genomes of Rhizobium sp., Sinorhizobium, Bradyrhizobium and Mesorhizobium

species carried chromosomal panCB genes. Only in A. tumefaciens C58 the panCB genes are localized in the linear chromosome, whereas in all other Rhizobiales harboring secondary chromosomes the panCB genes were located in www.selleckchem.com/products/netarsudil-ar-13324.html chromosome I. A bioinformatic analysis with MicrobesOnline operon predictions [22] indicates that panCB genes are organized as possible operons in most of the Rhizobiales examined in this work: all these predicted operons conserve the four nucleotide overlap between the panC TGA codon and the panB ATG codon observed in R. etli CFN42 (data not shown). In the genomes of Bradyrhizobium sp. BTAi1, Nitrobacter hamburgensis X14, Methylobacterium

extorquens AM1, Methylobacterium radiotolerans eFT-508 datasheet JCM2831 and Xantobacter autotrophicus Ry2, panC and panB are encoded in separate chromosomal loci, whereas in Methylobacterium nodulans ORS2060 panC is located in the chromosome and panB in plasmid pMNOD02. The Rhizobiales BI 10773 cell line phylogeny inferred from concatenated panC and panB genes was consistent with the phylogeny deduced from 10 concatenated housekeeping genes. The low bootstrap values obtained for some nodes of the panCB phylogeny might be due to the small number of informative characters in the alignments of only two genes (1 977 nucleotides). This is consistent with previous reports that state that trees from longer alignments obtained by the concatenation of genes encoding multiple-protein families have higher bootstrap support than trees inferred from genes encoding single proteins [23]. The phylogenetic relationships among Rhizobium species carrying panCB genes in plasmids with

their closest relatives, Agrobacterium and Sinorhizobium species, harboring panCB genes in Buspirone HCl the chromosome was also observed in neighbor-joining trees inferred from single panC and panB genes (data not shown). These data agree with the hypothesis that plasmid-encoded panCB genes are orthologs of the panCB genes located in chromosome. From these results, we propose that the presence of the panCB genes in plasmids in R. etli and R. leguminosarum species may be due to an intragenomic transfer event from chromosome to plasmid. The mechanism leading to the transfer of core genes from chromosome to plasmids could involve cointegration and excision events between the replicons, similar to rearrangements that have been visualized in S. meliloti [24]. The translocation of genes from chromosome to plasmids may be part of the complex evolution of multipartite genomes.

The difference between the cell types may reflect the fact that J774A.1 cells are phagocytic macrophages, and the A549 cells are non-phagocytic epithelial cells. Figure 3 Az inhibition of intracellular Francisella strains. After 22 hours, recovered bacterial counts were measured for F. philomiragia, F. novicida, and F. tularensis LVS infected cells (MOI 500).

A) J774A.1 cells infected with F. philomiragia, F. novicida, or F. tularensis LVS had more than 105 CFU/ml. Bacterial counts decreased for all strains as the Az concentrations increased and were near 0 CFU/ml at 5 μg/ml Az. selleck chemicals llc B) A549 cells infected with F. philomiragia, F. novicida, or F. tularensis

LVS had more than 105 CFU/ml at 0 μg/ml Az. Bacterial counts decreased at 0.1 and 5 μg/ml Az and were near 0 CFU/ml at 25 μg/ml Az. CFU counts from no Az treatment compared 0.1, 5, and 25 μg/ml Az treatment for all Francisella strains were significantly different (p-value < 0.005). To determine if Francisella bacteria counts were decreased due to Az concentrations or due to cell death, cellular lysis and apoptosis were measured by LDH released [19]. At 22 hours, cell cytotoxicity in non-infected A549 cells and A549 cells infected with F. novicida, F. philomiragia, and F. tularensis LVS remained below 20%. Non-infected LOXO-101 in vitro A549 cells along with F. philomiragia, F. novicida, and F. tularensis LVS-infected cells had a slightly increased cytotoxicity as Az concentrations increased (Table 3). Cellular apoptosis remained low with all Az doses. These results suggest the decreased Francisella counts were due to Az treatment and not due to bacterial release

during the experiment from apoptosis or cell lysis. Table 3 A549 cell cytotoxicity. Bacteria 0 μg/ml Az 0.1 μg/ml Az 1.0 μg/ml Az 2.5 μg/ml Az 5.0 μg/ml Az A549 cells 0 ± 3.0 2.9 ± 2.8 8.0 ± 4.0 18.3 ± 5.2 19.7 ± 9.6 F. novicida 0 ± 2.3 4.1 ± 5.0 3.3 ± 6.3 9.6 ± 5.4 17.8 ± 13.2 F. philomiragia 0 ± 1.3 0 ± 2.5 7.1 ± 4.6 1.7 ± 3.2 8.5 ± 4.1 F. tularensis LVS 0 ± 3.7 2.12 ± 5.0 4.6 ± 5.9 8.4 ± 5.1 5.2 ± 5.6 Using a LDH release assay, the cell cytotoxicity as a result of antibiotic and/or CYTH4 Francisella infection was determined and is indicated as a percentage (%) of total LDH released. Francisella LPS mutants Due to the potential for interaction of Az with LPS [9], four F. novicida transposon LPS O-antigen mutants were tested for their Az susceptibility: O-antigen of LPS (wbtA) biosynthesis of GdNAcAN, an O-antigen unit (wbtE), glycosylatransferase that elongates to form GalNAcAN tri-saccharides (wbtQ), and aminotransferase (wbtN) [10]. F. novicida LPS O-antigen mutants including wbtA, wbtE, wbtQ, and wbtN were shown to be less susceptible to Az by decreased zones of inhibition in comparison to the BI 6727 wild-type (p-value < 0.001) (Table 4). The MICs for Az against the F. novicida LPS-related transposon mutants wbtA, wbtE, wbtQ, and wbtN (MIC's > 3.0 μg/ml Az, EC50 > 0.

The part of the noise suppressed by dc bias has been interpreted as arising due to Nutlin-3a cost trapping-detrapping noise in the depletion region at the interface. The residual noise has been has been linked to the noise in the single Si NW, which

has the conventional 1/f VX-680 spectral power density with an estimated Hooge parameter γ H ≃ 10 − 8. Acknowledgements The authors thank Nanomission, Department of Science and Technology, Govt. of India for financial support as sponsored projects UNANST-II and Theme Unit of Excellence in Nanodevice Technology. References 1. Byon K, Tham D, Fischer JE, Johnson AT: Systematic study of contact annealing: ambipolar silicon nanowire transistor with improved performance. Appl Phys Lett 2007, 90:143513/1–143513/3.CrossRef 2. Goldberger J, Hochbaum AI, Fan R, Yang P: Silicon vertically integrated nanowire field effect transistors. Nano Lett 2006, 6:973–977.CrossRef 3. Cui Y, Wei Q, Park H, Lieber CM: Nanowire nanosensors for highly sensitive and selective detection of biological and chemical species. Science 2001, 293:1289–1292.CrossRef Crenolanib 4. Stern E, Klemic JF, Routenberg DA, Wyrembak PN, Turner-Evans DB, Hamilton AD, LaVan DA, Fahmy TM, Reed MA: Label-free immunodetection with CMOS-compatible semiconducting nanowires.

Nature 2007, 445:519–522.CrossRef 5. Bae J, Kim H, Dang CH, Zhang Y, Choi YJ, Nurmikko A, Wang ZL, Zhang Xiao-Mei: Si nanowire metal-insulator-semiconductor photodetectors as efficient light harvesters. Nanotechnology 2010, 21:095502/1–095502/5.CrossRef 6. Paladino E, DArrigo A, Mastellone A, Falci G: Decoherence times of universal two-qubit gates in the presence of broad-band noise. New J Physics 2011, 13:093037/1–093037/34.CrossRef 7. Wei C, Zhou X, Singh N, Rustagi SC, Lo GQ, Kwong D-L, Xiong Yong-Zhong: Investigation of Low-frequency noise in silicon nanowire MOSFETs in the subthreshold region. IEEE Electron Device Lett 2009, 30:668–671.CrossRef 8. McWhorter AL: Semiconductor Surface Physics. Edited by Kingston RH. Philadelphia:

University of Pennsylvania Press; 1957. 207–228 9. Peng KQ, Yan YJ, Gao SP, Zhu J: Synthesis of Liothyronine Sodium large-area silicon nanowire arrays via self-assembling nanoelectrochemistry. Adv Mater 2002, 14:1164–1167.CrossRef 10. Chakravorty M, Naik J, Das K, Prewett PD, Raychaudhuri AK: Temperature dependent resistivity of platinum-carbon composite nanowires grown by focused ion beam on SiO2/Si substrate. Microelectronic Eng 2011, 88:3360–3364.CrossRef 11. Norde H: A modified forward I-V plot for Schottky diodes with high series resistance. J Appl Phys 1979, 50:5052–5053.CrossRef 12. Scofield JH: ac method for measuring low-frequency resistance fluctuation spectra. Rev Sci Instrum 1987, 58:985–993.CrossRef 13.

parahaemolyticus 9 PVP-B ATCAAACTCAGGACATGCACCC     PVC-F TCCTGCACCTTGCTCTGCTCT prfC of V. cholerae 9 PVC-B ACCACGCTCTTTTTCCATTTCCAT     setRpF CGGCGGAGATGTTTTTGT setR 8 setRpR GTGCGCCAATGCTCAGTT     traC-F TGACGCTGTTTTCACCAACG

traC 8 traC-B GGCACGACCTTTTTTCTCCC     traI-F GCAAGTCCTGATCCGCTATC traI 8 traI-R CAGGGCATCTCATATGCGT     LEFTF3 GGTGCCATCTCCTCCAAAGTGC rumBA (VRIII) 39 RUMA CGAGCAATCCCCACATCAAG     HS1-F GGTTCAGGCGTCATCTT s043-traL This study HS1-R TCTCATCGGCACTCCA     HS2-F GTCGTTGCCAGCACTCA traA-s054 This study HS2-R CGCCAGAATGATTGGAGAT     HS3-F GGTGTACTGGAAGACCGG s073-traF This study HS3-R CAGGCAGCACTGAAAGG     HS4-F AGTGACCCAGGCATAGAC traN-s063 This study HS4-R GAAGAGGAAACAGATAACCC     E1 TTGCGGGAGATTATGCTC eex 43 E2 TGACCATCAATGAAGGTTG     T1 CATCTAGCGCCGTTGTTAATCAGGT traG 43 T2 ATCGCGATACTCAGCACGTCGTGAA     ctxA-F CGGGCAGATTCTAGACCTCCTG AMN-107 nmr ctxA 48 ctxA-R C646 mouse CGATGATCTTGGAGCATTCCCAC     L-TLH AAAGCGGATTATGCAGAAGCACTG tlh 47 R-TLH GCT ACTTTCTAGCATTTTCTCTGC     tdh-1 CCATCTGTCCCTTTTCCTGCC tdh 47 tdh-4c

CCACTACCACTCTCATATGC     VPTRH-L TTGGCTTCGATATTTTCAGTATCT trh 47 VPTRH-R CATAACAAACATATGCCCATTTCCG     P1 P505-15 TGCTGTCATCTGCATTCTCCTG circular ICEs 24 P2 GCCAATTACGATTAACACGACGG     *The primers were designed based on the corresponding gene sequences of SXT (GenBank: AY055428). Hotspot2. In addition to SXT or R391-specific molecular profiles in hotspot2 loci as previously reported [23], variable gene contents in HS2 were identified in eight ICEs characterized in this study (Figure 1). Previous studies indicated that most SXT/R391 ICEs contain mosA and mosT genes in HS2, which encode a novel toxin-antitoxin pair that promotes SXT maintenance by killing or severely inhibiting the growth of cells that have lost this Methane monooxygenase element [37]. However, the two genes were absent from the HS2 (1.3 kb) in six ICEs including ICEVchChn1, ICEVchChn3, ICEVchChn4, ICEVchChn5, ICEVchChn6 and ICEVpaChn1. These results are consistent

with those yielded from R391 and few other ICEs [10, 37]. Nevertheless, BLAST analysis of the HS2 (GenBank: KF411056-KF411060) in these six elements revealed that they contain two homologous genes (98% amino acid identity) to those that occur in the 3′-region of the HS2 in ICEVspPor2, possibly encoding additional anti-toxin component protecting against the loss of the ICEs [10]. It is thus interesting to study if these two genes could compensate for the mosAT loss in these elements. In this study, BLAST analysis also revealed that ICEValChn1 (GenBank: KF411061) contains the first two (orf45, orf46) of ten genes in the HS2 of R391. However, unlike R391, downstream of these two genes, ICEValChn1 also contains a gene with 98% amino acid sequence identity to a transposase of IS605 OrfB family of the Shewanella sp.

anthropi strains were isolated from samples of 19 patients admitted to

the Catanzaro University Hospital (Italy) Oncology O.U. Samples were taken as part of standard patient care and all procedures were approved by the local ethics committee at the Medical Faculty of the University “Magna Graecia” of Catanzaro, which are in compliance with Declaration of Helsinki (59th WMA General Assembly, Seoul, October 2008). During stay in hospital, all patients, which presented severe background disease, mainly neoplasia, showed mild clinical signs of sepsis. We therefore performed blood cultures by BacT/Alert 3D system (bioMèrieux, Clinical Diagnostics, France), detecting 18 isolates from 18 positive blood cultures drawn from the central venous catheter (CVC) and 5 isolates from positive catheter tip cultures (Table 1). The strains were conventionally identified by typical Gram stain morphology and biochemical testing (Vitek-2, bioMèrieux, ABT-737 purchase France). Antibiotic sensitivity was evaluated by Vitek System (bioMèrieux, France). To exclude Brucella misdiagnosis, the O. anthropi colonies of all isolates were tested with Brucella agglutinating

sera (Brucella spp., Brucella abortus and Brucella melitensis). Table 1 O. anthropi strains isolated from patients admitted to the Oncology O.U. Strain ID Patient ID Isolation location Date of isolation CZ1403 1 Blood 26/04/2011 CZ1424* 2 Blood selleck products 17/05/2011 CZ1427* 3 Blood 19/05/2011 CZ1425 4 Blood 20/05/2011 CZ1429* 3 Catheter tip 25/05/2011 CZ1433 5 Blood 06/06/2011 CZ1439 6 Blood 06/06/2011 CZ1442 7 Blood 09/06/2011 CZ1443* 2 Catheter tip 09/06/2011 CZ1449* 3 Catheter tip 11/06/2011 CZ1454 8 Blood 17/06/2011 CZ1458 9 Blood 20/06/2011 CZ1460 10 Blood 21/06/2011 CZ1474 Arachidonate 15-lipoxygenase 11 Blood 29/06/2011 CZ1476 12 Blood 29/06/2011 CZ1505 13 Catheter tip 07/07/2011 CZ1504* 14 Blood 08/07/2011 CZ1523* 14 Catheter tip 14/07/2011 CZ1532 15 Blood 15/07/2011 CZ1519 16 Blood 19/07/2011 CZ1541 17 Blood 20/07/2011 CZ1552 18 Blood 26/07/2011 CZ1573 19 Blood 24/08/2011 *strains isolated from the same patient. Rep-PCR-based DNA fingerprinting by the DiversiLab System For rep-PCR analysis, bacteria (23 clinical strains

of O. anthropi, in addition to O. anthropi ATCC49188T and O. intermedium LMG3301T, kind gifts from Dr. Fabien Aujoulat, Universitè Montpellier, France) were grown on Columbia blood agar; DNA was extracted from a 10-μl loopful of each O. anthropi colony, using an UltraClean Microbial DNA isolation kit (Mo Bio Laboratories, Carlsbad, CA). The extracted DNA was amplified using a DiversiLab Generic DNA fingerprinting kit (bioMèrieux, France), following the manufacturer’s instructions. DiversiLab Rep-PCR was performed according to Treviño M. et al., 2011 [13]. Briefly, 50 ng of genomic DNA, 2.5 U of AmpliTaq DNA polymerase, and 1.5 μl of 10× PCR buffer (Applied Biosystems, Foster City, CA) were added to the appropriate rep-PCR master mix to PF-6463922 supplier achieve a total of 25 μl.

PubMedCrossRef 6. Progulske-Fox A, Kozarov E, Dorn B, Dunn W Jr, Burks J, Wu Y: Porphyromonas gingivalis virulence factors and invasion of cells of the cardiovascular system. J Periodontol

Selleckchem BI 10773 Res 1999, 34:393–399.CrossRef 7. Bartold PM, Marshall RI, Haynes DR: Periodontitis and rheumatoid arthritis: a review. J Periodontol 2005, 76:2066–2074.PubMedCrossRef 8. Leon R, Silva N, Ovalle A, Chaparro A, Ahumada A, Inhibitor Library molecular weight Gajardo M, Martinez M, Gamonal J: Detection of Porphyromonas gingivalis in the amniotic fluid in pregnant women with a diagnosis of threatened premature labor. J Periodontol 2007, 78:1249–1255.PubMedCrossRef 9. Mattila KJ, Pussinen PJ, Paju S: Dental infections and cardiovascular disease: a review. J Periodontol 2005, 76:2095–2088.CrossRef 10. Wang Q, Zhou X, Huang D: Role for Porphyromonas gingivalis in the progression of atherosclerosis. Med Hypotheses 2009, 72:71–73.PubMedCrossRef 11. McKee AS, McDermid AS, Baskerville A, Dowsett AB, Ellwood DC, Marsh PD: Effect of hemin on the physiology and virulence of Bacteroides https://www.selleckchem.com/products/VX-765.html gingivalis . Infect Immun 1986, 52:349–355.PubMed 12. Olczak T, Simpson

W, Liu X, Genco CA: Iron and heme utilization in Porphyromonas gingivalis . FEMS Microbiol Rev 2005, 29:119–144.PubMedCrossRef 13. Liu X, Olczak T, Guo HC, Dixon DW, Genco CA: Identification of essential amino acid residues required for hemoprotein utilization in the Porphyromonas gingivalis heme receptor HmuR. Infect Immun 2006, 74:1222–1232.PubMedCrossRef 14. Olczak T: Analysis of conserved glutamate residues in Porphyromonas gingivalis heme receptor HmuR: toward a further understanding of heme uptake. Arch Microbiol 2006, 186:393–402.PubMedCrossRef 15. Olczak T, Dixon DW, Genco CA: Binding specificity of the Porphyromonas gingivalis heme and hemoglobin receptor HmuR, gingipain K, and gingipain R1 for heme, porphyrins,

and metalloporphyrins. J Bacteriol 2001, 183:5599–5608.PubMedCrossRef 16. Simpson W, Olczak T, Genco CA: Characterization and expression of HmuR, a TonB-dependent hemoglobin receptor of Porphyromonas gingivalis . J Bacteriol 2000, 182:5737–5748.PubMedCrossRef 17. Lewis JP, Plata K, Fan Y, Rosato A, Anaya C: Transcriptional organization, regulation and role of the Porphyromonas gingivalis W83 hmu haemin-uptake locus. Microbiology Selleckchem Temsirolimus 2006, 152:3367–3382.PubMedCrossRef 18. Olczak T, Siudeja K, Olczak M: Purification and initial characterization of a novel HmuY protein from Porphyromonas gingivalis expressed in Eschericha coli and insect cells. Protein Expr Purif 2006, 49:299–306.PubMedCrossRef 19. Olczak T, Sroka A, Potempa J, Olczak M: Porphyromonas gingivalis HmuY and HmuR – further characterization of a novel mechanism of heme utilization. Arch Microbiol 2008, 183:197–210.CrossRef 20. Wojtowicz H, Wojaczynski J, Olczak M, Kroliczewski J, Latos-Grazynski L, Olczak T: Heme environment in HmuY, the heme-binding protein of Porphyromonas gingivalis . Biochem Biophys Res Commun 2009, 383:178–182.PubMedCrossRef 21.

These conditioning regimens prior to allogenic or autologous HSC transplantation are used to treat a large number of malignant diseases such as leukemia and some solid tumors, as well as genetic diseases such as immune deficiency syndromes [4–7]. Other combinations associate LY2874455 clinical trial busulfan with thiotepa. More recently, less myoloablative

combinations with fludarabine (BuFlu) have shown efficacy while offering lower extrahematological toxicity [8, 9]. According to the Summary of Product Characteristics (SPC), Busulfan (Busilvex®) is administered intravenously (IV) at a recommended dose of 0.8 mg/kg in adults and 0.8–1.2 mg/kg (depending on bodyweight) in pediatric patients [3]. It is administered by means of a 2-h infusion every 6 h for 4 consecutive days (giving a total of 16 doses). Because of its highly predictable linear pharmacokinetics, once-daily administrations are under evaluation in adults [10]. Busulfan is provided as a 6 mg/mL concentrate and once it has been reconstituted in the form of a GDC-0941 supplier 0.55 mg/mL solution, the stability data provided by Pierre Fabre Laboratories are 8 h at 20 ± 5 °C (room temperature [RT]) or 12 h at 2–8 °C followed by 3 h at RT. More recently, a German study reported a period of stability of 36 h at a temperature between 13 and 15 °C for the same solutions

diluted to a 0.5 mg/mL dose and prepared in polypropylene (PP) bags or glass bottles [11, 12]. Busulfan undergoes a hydrolysis phenomenon in aqueous media, giving rise to methanesulphonic acid and tetrahydrofuran

(THF) [13]. A precipitation phenomenon was also identified during these studies [11]. The short shelf life specified in the SPC combined with the administration regimen of every 6 h for 4 consecutive days poses organizational problems for chemotherapy preparation, particularly at the end of the week. The purpose of our study was to investigate the stability of busulfan injection solution (Busilvex®) diluted in 0.9 % sodium chloride (NaCl) to a concentration of 0.55 mg/mL (the recommended concentration for administration) in three different containers: PP syringes, polyvinyl Inositol oxygenase chloride (PVC) bags, and glass bottles, when stored at three different temperatures (2–8, 13–15, and 20 ± 5 °C). We monitored changes in the busulfan content of this solution, its pH, and its osmolality over time, and sought to understand the phenomena causing the busulfan content to decrease. 2 Materials and Methods 2.1 Materials and Reagents Busulfan (Fig. 1) (Fluka, Steinheim, Germany; purity ≥99 %) was used to 4SC-202 mouse produce the series of standard solutions for calibration and the quality controls. Diethyldithiocarbamate (Fig. 1) (Sigma-Aldrich, St Louis, MO, USA) was used to prepare the derivatization solution each day. The Busilvex® used for the preparations was supplied by Pierre Fabre Oncologie, Boulogne, France.

glutamicum::dld(pEKEx3) formed about half as much biomass as strains WT(pEKEx3), WT(pEKEx3-dld), and ::dld(pEKEx3-dld) indicating that only L-lactate is utilized in the absence of Dld while strains possessing Dld utilized both L- and D-lactate for growth (data not shown). Dld activities under various growth conditions The specific quinone-dependent D-lactate dehydrogenase activity was determined in crude extracts of C. glutamicum ATCC 13032 grown under different conditions. Neither the addition of L-lactate nor of D-lactate to complex medium affected the specific https://www.selleckchem.com/products/ly2835219.html activity of Dld (Figure 2). Dld activities were also

similar after growth in CgXII minimal medium with various carbon sources (Figure 2). Thus, the comparable Dld activities in C. glutamicum cells grown in different media suggested that dld is expressed constitutively. Figure 2 Specific activities of the quinone-dependent D-lactate dehydrogenase Dld in crude extracts of C. glutamicum WT grown in different media.

The Copanlisib molecular weight values represent means and standard deviations of at least three independent cultivations in LB EPZ5676 complex medium without or with 100 mM L-lactate or 100 mM D-lactate or in CgXII mineral medium containing either 100 mM glucose, 100 mM L-lactate, 100 mM D-lactate or 100 mM pyruvate as carbon source. DNA microarray analysis of D-lactate specific gene expression changes Comparative transcriptome analysis was performed for C. glutamicum cells grown in LB with/without this website added D-lactate as well as in CgXII minimal medium with DL-lactate or L-lactate as sole carbon sources. These carbon source combinations were chosen to avoid secondary effects in comparisons with non-gluconeogenic carbon sources such as glucose and because L-lactate specific gene expression patterns were known [24]. Neither the addition of D-lactate to LB nor the presence of D-lactate in minimal medium affected dld expression. However, upon addition of D-lactate to LB medium eight genes showed altered expression levels as compared to the absence of D-lactate. Of these, five genes showed higher and three genes lower RNA levels in the presence of D-lactate. Growth

in DL-lactate minimal medium was characterized by lower expression of fourteen genes as compared to growth in L-lactate. As most of these genes encoded ATPase subunits or ribosomal proteins this expression pattern likely reflects the lower growth rate in DL-lactate than in L-lactate minimal medium. Heterologous expression of dld from C. glutamicum ATCC 13032 in C. Efficiens Comparison of the genome of C. glutamicum ATCC 13032 with the genomes of closely related species revealed that C. glutamicum R, C. efficiens, C. jeikeium and C. urealytikum do not possess a protein homologous to Dld (Figure 3). C. efficiens has been described to be unable to assimilate D-lactate [40]. To test whether the absence of a gene homologous to dld resulted in the inability of C. efficiens to grow in D-lactate minimal medium, C.

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the manuscript. MJK helped to conceive the study, participated in the experimental design and coordination, and helped to draft the manuscript. Both have given final approval to this work and have no conflicts of interest to report.”
“Background Brucella is the etiologic agent of brucellosis, a worldwide zoonosis that affects a broad range of mammals, including Demeclocycline humans [1]. Brucella is considered as a facultative intracellular pathogen that enters various cell types during the infection process, including macrophages and epithelial cells, and ultimately survives and multiplies inside these cells [2]. After internalization, intracellular Brucella resides within a vacuole (BCV for Brucella-containing vacuole) that interacts with early endosomes [3] and then transiently acquire markers of late endosomes such as LAMP1. In epithelial cells and macrophages, non-opsonized bacteria replicate finally in a compartment characterized by the presence of endoplasmic reticulum (ER) markers [[4–7]].