Body composition was directly measured in the supine position by Dual emission X-ray absorptiometry (DEXA). Fat distribution was indirectly measured by LY2603618 molecular weight the ratio of waist and hip circumferences. The waist circumference was measured at the end of a normal expiration and at the mid-point between the bottom rib and the superior iliac spine. Hip circumference was measured on a horizontal plane at the site of maximum extension of the buttocks [16]. Study procedure

Subjects participated in 5 visits, starting with an incremental exercise test to determine maximal oxygen consumption ( ) in trained men and peak oxygen consumption ( ) in untrained men. One week later, they randomly performed the experiment, consisting of two 4-week phases with a 4-week washout between the treatments. In the experimental phases they were supplemented Romidepsin chemical structure with either PLA or CAJ (3.5 ml/kg BM/day) continuously for 4 weeks. Before and after each phase, they performed high-intensity exercise by cycling at 85% for 20 min in trained subjects and 85% in untrained subjects. They fasted

overnight before each exercise session. The final dose of CAJ / PLA was taken the day before the exercise session after each phase. Venous blood samples were taken before and after the exercise to determine glucose, insulin and vitamin C concentrations and lipid profile, including total cholesterol (TC), high-density lipoprotein (HDL), low-density lipoprotein (LDL), and triglycerides (TG). During the exercise sessions, expired-air samples were collected to determine substrate utilization (CHO and fat oxidation rates and CHO and fat contribution to total EE) and EE. Throughout the experimental period the subjects were instructed not to change their diets or exercise routines. Incremental or exercise test Subjects began the test by warming up with free Foretinib workload (0 watt) cycling for 2 minutes. They then started with a workload at 30–50 watts depending on their fitness status.

Workloads were STK38 increased by 20–30 watts every 3 minutes until they reached the criteria establishing or ; included possession of maximum symptoms of dyspnea (9-10) and fatigue (18-20), determined by rating of perceived dyspnea (RPD) and rating of perceived exertion (RPE) scales; inability to maintain a cycling speed of at least 60 rpm; an increase of heart rate (HR) to predicted HRmax (220 – age); and steady or falling VO2. Expired-air samples, oxygen saturation, and HR were recorded throughout the test, and the dyspnea and fatigue symptoms were inquired of the subjects at the end of each workload. Electrocardiography was monitored throughout the exercise experiments.

5 ml 2 mM dithiothreitol in 50 mM Tris-Cl, pH8. The suspended bacteria were disrupted in a FastPrep220A at 4 m/sec for 3 cycles of 20 sec in Lysing Matrix B (0.1 mm silica beads), with cooling on ice between cycles. The resulting cell-extracts were then clarified at 4000 g for 4 min this website using a bench centrifuge and BMS345541 filter-sterilised through 0.2 μm pore cellulose acetate filters (Sartorius Minisart). Each clarified cell extract was desalted through Pharmacia PD-10 columns according to the manufacturer’s instructions; with the exception that 3.2 ml (not 3.5 ml) protein fraction was collected. For equilibrating, desalting and eluting using PD-10, 50 mM Tris-Cl,

pH8 was used. Phosphatase assays were conducted using 0.4 mM substrates at 37°C, as described previously [33] although the reaction volume used was 120 μl and was stopped with 30 μl malachite green reagent. No precipitates were formed so the entire assay was performed in ELISA plate wells. Inorganic phosphate present in each well was calculated by reading the OD against a standard curve. Enzyme activity was

then calculated by subtracting the phosphate formed in wells with cell extract and substrate, from phosphate formed in corresponding wells with cell extract but without substrate. Results Bioinformatics analysis There are four genes in the M. tuberculosis genome that encode proteins with significant homology to IMPases. All four M. tuberculosis proteins are equally distant SP600125 cell line from the human IMPase (PDB structure 1IMA; 22-30% identity, 37-46% similarity) [34] and the aligned amino acid sequences are shown in Figure

1A. The four proteins are only as similar to each other, as to the human protein (27-32% identity, 36-44% similarity). Figure 1 Alignment of IMPases. The M. tuberculosis Ribonucleotide reductase H37RvIMPases were aligned using ClustalW. (A) Complete sequences. Motifs shown in bold; (B) Prosite motifs: ‘*’ identical residues in all sequences; ‘:’ conserved substitutions; ‘.’ semi-conserved substitutions. Sequences were obtained from http://​genolist.​pasteur.​fr/​TubercuList/​. Reported Prosite motifs are 1 (N-terminal; PS00629): [FWV]-x(0,1)- [LIVM]-D-P- [LIVM]-D- [SG]- [ST]-x(2)- [FY]-x- [HKRNSTY]; and 2 (C-terminal; PS00630): [WYV]-D-x- [AC]- [GSA]- [GSAPV]-x- [LIVFACP]- [LIVM]- [LIVAC]-x(3)- [GH]- [GA]. Residues that are not encompassed by these motifs are in bold italics. Arrows indicate putative metal binding aspartate and isoleucine residues reported for human IMPase [55]. The underlined residue shows the aspartate mutated in this study, which is equivalent to mutations introduced into the E. coli and human proteins (see main text). These four genes are generally conserved in other actinomycete genomes, with for example, apparent orthologs in Mycobacterium avium, Mycobacterium smegmatis, and Corynebacterium glutamicum (data not shown). M. leprae, which has many pseudogenes, has no functional impA.

mimicus lineage after the lineage evolved from a progenitor of V. mimicus/V. see more cholerae (Figure 2). These iterations are supported by strong bootstrap support calculations. A close evolutionary relationship for Vibrio sp. RC586 and V. mimicus is also supported by shorter evolutionary distances between the Vibrio sp. RC586 and V. mimicus strains (see Additional files 8 and 9). The evolutionary

distance of all genomes used in this study from V. cholerae BX 330286, a putative progeny of the progenitor of the 7th pandemic clade [17, 24], is shown in Additional file 10. Virulence Factors Both Vibrio sp. RC586 and Vibrio sp. RC341 genomes encode several virulence factors found in toxigenic and non-toxigenic V. cholerae and V. mimicus. These include the toxR/toxS virulence regulators, multiple hemolysins and lipases, VSP-I and II, and a type 6 secretion system. Both VSP islands are also present in pathogenic strains of the seventh pandemic clade [25]. Although neither genome encodes CTXΦ phage, the major virulence factor

encoding the cholera toxin (CT) that is responsible for the profuse secretory diarrhea caused by toxigenic V. cholerae and V. mimicus, both genomes do have homologous sequences of the chromosomal selleckchem attachment site for this phage. Although these genomes do not encode TcpA, the outer membrane protein that CTXΦ attaches to during its infection cycle and ToxT, involved in CTXΦ replication and activation, they do encode several other mechanisms necessary for the complete CTXΦ life cycle and both CT production and translocation, including TolQRA, inner membrane proteins involved

in CTXΦ attachment to the cell, XerCD tyrosine recombinases, which catalyze recombination between CTXΦ and the host genome, LexA, involved in CTXΦ expression, and EspD, involved in the secretion of the CTXΦ virion and CT translocation into the extracellular environment. Neither Vibrio sp. RC341 nor Vibrio sp. RC586 encode VPI-1 or VPI-2, but Vibrio sp. RC341 encodes one copy of both VSP-I (VCJ_003466-VCJ_003480) and VSP-II (VCJ_000310 to VCJ_000324) and Vibrio sp. RC586 encodes one copy of VSP-I (VOA_002906-VOA_002918). However, neither of these strains encodes complete ADP ribosylation factor VSP islands, but rather Ulixertinib cost variants of canonical VSP islands. Incomplete VSP islands have been frequently found in environmental V. cholerae and V. mimicus isolates [26] [Taviani et al, unpublished]. The toxR/toxS virulence regulators, hemolysins, lipases, and type 6 secretion system are present in all pathogenic and non-pathogenic strains of V. cholerae and both VSP islands are present in pathogenic strains of the seventh pandemic. Presence of these virulence factors in V. cholerae genomes sequenced to date, as well as their divergence consistent with the conserved core of Vibrio sp. RC341 and Vibrio sp. RC586, suggests that they comprise a portion of the backbone of many Vibrio species.

4.3.2 Targeting Survivin Many studies have investigated various approaches targeting Survivin for cancer intervention. One example is the use of antisense oligonucleotides. Grossman et al was among the first to demonstrate the use of the antisense approach in human melanoma cells. It was shown that transfection of anti-sense Survivin into YUSAC-2 and LOX malignant melanoma cells resulted in spontaneous learn more apoptosis

in these cells [90]. The anti-sense approach has also been applied in head and neck squamous cell carcinoma and reported to induce apoptosis and sensitise these cells to chemotherapy [91] and in medullary thyroid carcinoma cells, and was found to inhibit growth and proliferation of these cells [92]. Another approach in targeting Survivin is the use of siRNAs, which have been shown to downregulate Survivin and diminish radioresistance in pancreatic cancer cells [93], to inhibit proliferation and induce apoptosis in SPCA1 and SH77 human lung adenocarcinoma cells [94], to suppress Survivin expression, inhibit cell proliferation and enhance apoptosis in SKOV3/DDP ovarian cancer cells [95] as well as to enhance the radiosensitivity selleck chemicals llc of human non-small cell lung cancer cells [96]. Besides, small molecules

antagonists of Survivin such as cyclin-dependent kinase inhibitors and Hsp90 inhibitors and gene therapy have also been attempted in targeting Survivin in cancer therapy (reviewed by Pennati et al., 2007 [97]). 4.3.3 Other IAP antagonists Other IAP antagonists include peptidic and non-peptidic small molecules, which act

as IAP inhibitors. Two cyclopeptidic Smac mimetics, 2 and 3, which were found to bind to XIAP and cIAP-1/2 and restore the activities of caspases- 9 and 3/-7 inhibited by XIAP were amongst the many examples [98]. On the other hand, SM-164, a non-peptidic IAP inhibitor was reported to strongly enhance TRAIL activity by concurrently targeting XIAP and cIAP1 [99]. 4.4 Targeting caspases 4.4.1 Caspase-based Ribonucleotide reductase drug therapy Several drugs have been designed to synthetically activate caspases. For example, Apoptin is a caspase-inducing agent which was initially derived from chicken click here anaemia virus and had the ability to selectively induce apoptosis in malignant but not normal cells [100]. Another class of drugs which are activators of caspases are the small molecules caspase activators. These are peptides which contain the arginin-glycine-aspartate motif. They are pro-apoptotic and have the ability to induce auto-activation of procaspase 3 directly. They have also been shown to lower the activation threshold of caspase or activate caspase, contributing to an increase in drug sensitivity of cancer cells [101]. 4.4.

Can J Bot 84:1794–1805 Copanlisib solubility dmso Matheny PB, Aime MC, Bougher NL et al (2009) Out of the Paleotropics? Historical biogeography and diversification of the cosmopolitan ectomycorrhizal mushroom family Inocybaceae. J Biogeogr 36:577–592 Mayden RL (1997) A hierarchy of species concepts: the denoument in the saga of the species problem. In: Claridge MF, Dawah HA, Wilson MR (eds) Species: the units of diversity. Chapman and Hall, London, pp 381–423 McLaughlin DJ, Frieders EM, Lü H (1995) A microscopist’s view of heterobasidiomycete phylogeny. Stud Mycol 38:91–109 McLaughlin DJ, Hibbett DS, Lutzoni F et al (2009) The search for the fungal tree of life. Trends Microbiol 17:488–497PubMed Miller OK

Jr (1971) The relationship of cultural Bcr-Abl inhibitor characters to the taxonomy

of the agarics. In: Petersen RH (ed) Evolution in higher basidiomycetes. The University of SGC-CBP30 molecular weight Tennessee Press, Knoxville, pp 197–215 Miller OK Jr, Horak E (1992) Observations on the genus Torrendia and a new species from Australia. Mycologia 84:64–71 Miller OK Jr, Miller HH (1988) Gasteromycetes – Morphological and developmental features with keys to the orders, families, and genera. Mad River, Eureka Moncalvo J-M (2005) Molecular Systematics: major fungal phylogenetic groups and fungal species concepts. In: Xu J (ed) Evolutionary genetics of fungi. Horizon Bioscience, Norfolk, pp 1–33 Moncalvo J-M, Vilgalys R, Redhead SA et al (2002) One hundred and seventeen

clades of euagarics. Mol Phylogenet Evol 23:357–400PubMed Moore RT (1985) The challenge of the dolipore/parenthosome septum. In: Moore D, Casselton LA, Wood 4-Aminobutyrate aminotransferase DA et al (eds) Developmental biology of higher fungi. Cambridge University Press, Cambridge, pp 175–212 Moore RT (1997) Evolutionary advances in the higher fungi. Antonie Van Leeuwenhoek 72:209–218PubMed Moser M (1983) Die Röhrlinge und Blätterpilze (Polyporales, Boletales, Agaricales, Russulales). In: Gams H (Hrg.) Kleine Kryptogamenflora, Band II b/2. Basidiomyceten, 2. Teil, 5. Aufl. Gustav Fischer Verlag, Stuttgart, pp 1–532 Mueller GM (1992) Systematics of Laccaria (Agaricales) in the continental United States and Canada, with discussions on extralimital taxa and descriptions of extant types. Fieldiana Botany New Series 30:1–158 Mueller GM, Wu QX, Huang YQ et al (2001) Assessing biogeographic relationships between North American and Chinese macrofungi. J Biogeogr 28:271–281 Mueller GM, Bills GF, Foster MS (2004) Biodiversity of fungi, inventory and monitoring methods. Elsevier Academic Press, Amsterdam Mueller GM, Schmit JP, Leacock PR et al (2007) Global diversity and distribution of macrofungi. Biodivers Conserv 16:37–48 Müller WH, Stalpers JA, Van Aelst AC et al (2000) The taxonomic position of Asterodon, Asterostroma and Coltricia inferred from the septal pore cap ultrastructure.

Similar to most cation diffusion facilitator (CDF) proteins, DR1236 has six putative transmembrane domains (TMDs) http://​www.​ch.​embnet.​org/​software/​TMPRED_​form.​html. The most conserved region of the buy ATM Kinase Inhibitor CDF protein is the TMD region, which is probably involved in metal transfer

[14]. Sequence alignment was performed with the CLUSTAL W program available on the EMBL web page http://​www.​ebi.​ac.​uk. The alignment Sp1552 and DR1236 revealed the presence of highly conserved sequences in metal transfer regions III and VI (Figure 1). Moreover, the DXXXD motif, which is conserved in the manganese efflux protein, was also present in DR1236 (224 DAGVD 230). Figure 1 Sequence alignment of the two manganese efflux proteins. DEIRA, Deinococcus radiodurans R1; STRPN, Streptococcus pneumoniae. The metal transfer regions III and VI are boxed. Identical amino acids and similar amino acids are denoted by black and gray backgrounds, respectively. mntE is essential for the manganese resistance of D. radiodurans To confirm the specific substrate and roles of DR1236 in D. radiodurans, the null mutant of dr1236 (mntE – ) and wild-type revertant mntE strains were constructed (Figure 2). Metals including manganese are essential yet potentially toxic to bacteria [15]. Supplementation

with certain metal ions can inhibit the growth of an exporter system mutant [16, 17]; therefore, this phenotype is used to verify certain mutants. In this study, wild-type R1 and dr1236 (mntE – ) were grown on TGY plates overlaid with discs saturated with 10 μL Capmatinib cost of different metal ion solutions (1 M) containing manganese, magnesium, cobalt, calcium, copper, zinc, nickel, or iron ions. As shown in Figure 3A/B, the growth of the

mntE – mutant was strongly inhibited by the manganese ions, but the mutant grew normally in the presence of other cations. Moreover, the wild-type revertant showed a growth phenotype similar to that of R1, indicating that growth inhibition of the mntE – mutant was due to the interruption of dr1236. Figure 2 mntE – mutant construction and verification by PCR. (A) Ethidium-bromide-stained agarose gel illustrating that the mutant carries a homozygous deletion of dr1236::aadA. these Lane 1, mntE – mutant; lane 2, R1; lane 3, DNA marker. IBET762 Primers M1/M4 were used for PCR. (B) Verification of wild-type revertant mntE by PCR. Lane 1, DNA marker; lane 2, R1; lane 3, revertant mntE. Primers M5/M6 were used for PCR. Figure 3 Manganese sensitivity assay for wild-type R1 and the mntE – mutant. (A) Wild-type R1 (white bars), mntE – (black bars), and WT revertant (gray bars) were cultured on TGY plates overlaid with filter discs saturated with 1 M solutions of various cations. The zone of inhibition was measured from the edge of the disc after three days. *P < 0.01. ND, not determined. (B) The inhibition zone of R1 and mntE – . Cells were cultured on TGY plates overlaid with filter discs saturated with 1 M manganese chloride.

Open Access This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any

noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. Electronic supplementary material Below is the link to the electronic supplementary material. Supplementary material 1 (PDF 275 kb) References 1. Cobo J, Miguel LGS, Euba G, et al. Early prosthetic joint infection: outcomes with debridement and implant retention Geneticin followed by antibiotic therapy. Clin Microbiol Infect. 2011;17:1632–7.PubMedCrossRef 2. Vilchez F, Martínez-Pastor JC, Garcia-Ramiro S, et al. Outcome and predictors of treatment failure in early post-surgical prosthetic joint infections S63845 manufacturer due to Staphylococcus aureus treated with debridement. Clin Microbiol Infect. 2011;17:439–44.PubMedCrossRef 3. Zimmerli W, Widmer AF, Blatter M, Frei R, Ochsner PE. Role of rifampin for treatment of orthopedic implant-related staphylococcal infections: a randomized controlled trial. Foreign-Body buy Dorsomorphin infection (FBI) Study Group. JAMA. 1998;279:1537–41.PubMedCrossRef 4. Lora-Tamayo J, Murillo O, Iribarren JA, et al. A large multicenter study of methicillin susceptible- and methicillin resistant-Staphylococcus aureus prosthetic joint infections managed with

implant retention. Clin Infect Dis. 2012;56:182–94.PubMedCrossRef 5. Senneville E, Joulie D, Legout L, et al. Outcome and predictors of treatment failure in total hip/knee prosthetic joint infections due to Staphylococcus aureus. Clin Infect Dis. 2011;53:334–40.PubMedCentralPubMedCrossRef 6. Bernard L, Legout L, Zürcher-Pfund L, et al. Six Phosphatidylinositol diacylglycerol-lyase weeks of antibiotic treatment is sufficient following surgery for septic arthroplasty. J Infect. 2010;61:125–32.PubMedCrossRef 7. Livermore DM. Linezolid in vitro:

mechanism and antibacterial spectrum. J Antimicrob Chemother. 2003;51(Suppl 2):ii9–16.PubMed 8. MacGowan AP. Pharmacokinetic and pharmacodynamic profile of linezolid in healthy volunteers and patients with Gram-positive infections. J Antimicrob Chemother. 2003;51(Suppl 2):ii17–25.PubMed 9. Kutscha-Lissberg F, Hebler U, Muhr G, Köller M. Linezolid penetration into bone and joint tissues infected with methicillin-resistant staphylococci. Antimicrob Agents Chemother. 2003;47:3964–6.PubMedCentralPubMedCrossRef 10. Baldoni D, Haschke M, Rajacic Z, Zimmerli W, Trampuz A. Linezolid alone or combined with rifampin against methicillin-resistant Staphylococcus aureus in experimental foreign-body infection. Antimicrob Agents Chemother. 2009;53:1142–8.PubMedCentralPubMedCrossRef 11. Gandelman K, Zhu T, Fahmi OA, et al. Unexpected effect of rifampin on the pharmacokinetics of linezolid. In silico and in vitro approaches to explain its mechanism. J Clin Pharmacol. 2011;51:229–36.PubMedCrossRef 12. Egle H, Trittler R, Kümmerer K, Lemmen SW. Linezolid and rifampin: drug interaction contrary to expectations? Clin Pharmacol Ther.

These mutations, as well as their Miki and Keio collection counterparts from NBRP (NIG, Japan): E. coli [18, 19] were subsequently transduced into FB8 hns::Sm derivative strains, using P1vir phage. When required, antibiotics were added: ampicillin (100 μg ml-1), streptomycin (10 μg ml-1), kanamycin (40 μg ml-1), tetracycline (15 μg ml-1). Table 1 Bacterial strains and plasmids

used in this study Strain or plasmid Genotype or description Reference or source Strains     JD21162 KP7600 (F- lacIQ lacZdeltaM15 galK2 galT22 lambda- in (rrnD-rrnE)1, W3110 derivative) ydeP ::Km [19] JD24946 KP7600 (F- lacIQ lacZdeltaM15 galK2 galT22 lambda- in (rrnD-rrnE)1, W3110 derivative) yhiM ::Km [19] JD25275 KP7600 (F- lacIQ lacZdeltaM15 galK2 galT22 lambda- in (rrnD-rrnE)1, W3110 derivative) hdeA ::Km [19] JD26576 KP7600 (F- lacIQ lacZdeltaM15 galK2 galT22 lambda- in (rrnD-rrnE)1, W3110 S63845 molecular weight derivative) ydeO::Km [19] JD27509 KP7600 (F- lacIQ lacZdeltaM15 galK2 galT22 lambda- in (rrnD-rrnE)1, W3110 derivative) dps ::Km [19] JW5594 BW25113 (rrnB ΔlacZ4787 HsdR514 Δ(araBAD)567 Δ(rhaBAD)568 rph-1) ΔaslB ::Km [18] JW2366 BW25113 (rrnB ΔlacZ4787 HsdR514 Δ(araBAD)567 Δ(rhaBAD)568 rph-1) ΔevgA ::Km [18] EP247 W3110 cadC1::Tn10 [41] FB8 Wild type [42] BE1411 FB8 hns::Sm [43] BE2823 FB8 hns::Sm ΔrcsB ::Km [6] BE2825 FB8 hns::Sm ΔhdfR ::Tet This study

BE2826 FB8 hns::Sm dps ::Km FB8 hns::Sm × P1 JD27509 BE2827 FB8 hns::Sm rpoS 359 click here ::Km This study BE2828 FB8 hns::Sm yhiM ::Km FB8 hns::Sm × P1 JD24946 BE2829 FB8 hns::Sm ΔevgA ::Km FB8 hns::Sm × P1 JW2366 BE2830 FB8 hns::Sm ΔaslB ::Km FB8 hns::Sm × P1 JW3772 BE2831 FB8 hns::Sm ydeP ::Km FB8 hns::Sm × P1 JD21162 BE2832 FB8 hns::Sm ydeO ::Km FB8 hns::Sm × P1 JD26576 BE2836 FB8 hns::Sm ΔhdeA ::Km FB8 hns::Sm × P1 JD25275 BE2837 FB8 hns::Sm ΔadiY ::Tet This study BE2939 FB8 hns::Sm cadC1::Tn10

FB8 hns::Sm × P1 EP247 Plasmids     pDIA640 pet22b ::hdfR with C terminal His tag This study pDIA642 pet16b ::rcsB D56E with N terminal His tag [6] pDIA645 pet22b ::gadE with C terminal His Phosphatidylinositol diacylglycerol-lyase tag [6] pDIA646 pet16b ::adiY with N terminal strep tag This study Resistance to low pH The experiment was performed at least twice, as previously described [6]. RNA preparation and Real-time quantitative RT-PCR The experiment was performed twice, as previously described [6]. Primers used in real-time quantitative RT-PCR experiments are listed in Additional file 1. Protein purification H-NS-His6 was purified as previously described [20]. Recombinant proteins HdfR-His6, His6-RcsBD56E, GadE-His6 and Strep-AdiY were purified as previously described [6]. Gel mobility shift assays Gel shift assays were performed with 0.1 ng [γ32P]-labelled probe DNA with purified HdfR-His6, His6-RcsBD56E (mimicking selleck kinase inhibitor phosphorylated and activated RcsB), GadE-His6 and Strep-AdiY proteins as previously described [6, 10].

data). (PDF 284 kb). (PDF 284 KB) Additional file 2 Table S3.: List of Brucella DNA samples tested with CUMA. DNA samples came from the following institutions, Louisiana State University (LSU), California Department of Health Services (CDHS), U.S. Armed Forces Institute of Pathology (AFIP), Alaska Public Health

Laboratory (APHL), Brigham Young University (BYU), U.S. Centers for Disease Control (CDC), USDA-National Animal Disease Center (NADC), and the Arizona Department of Health Services (ADHS). Samples with a species name in the branch column were genotyped as that species using assays in (Foster Sepantronium clinical trial et al. 2008) but gave all ancestral SNP alleles in our assays. Assays for B. abortus in blue B. melitensis in pink, and B. suis/canis in green, which correspond to the branches in Figure 1. The 85 samples also run in the MIP assay have an asterisk, except for 3 samples not run on CUMA. Samples likely mislabeled, due to incorrect branch assignment based on species/biovar, are VX 770 highlighted in yellow. (PDF 135 kb). (PDF 135 SP600125 in vitro KB) Additional file 3 Table S1.: List of 28 whole genomes used for in silico comparisons to SNP alleles from MIP assay. (PDF 62 kb). (DOCX 86 KB) Additional file 4 Table S2.: List of Brucella isolates used in 17 CUMA assays, including isolate name,

species, and biovar when known or applicable and the SNP allele for each assay. (PDF 44 kb). (DOCX 43 KB) References 1. Cloeckaert A, Vizcaino N: DNA polymorphism and taxonomy of Brucella species. In Brucella: Molecular and Cellular Biology. Edited by: Lopez-Goni I, Moriyon I. Horizon Bioscience, Norfolk, UK; 2004:1–24. 2. Verger JM, Grimont F, Grimont PAD, Grayon M: Brucella, a monospecific genus as shown by deoxyribonucleic acid hybridization. Int J Syst Bacteriol 1985, 35:292–295.CrossRef

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