coli EP-CD4 (cadC::Tn10, cadA’::lacZ, ΔlysP). In a lysP – background, wild-type CadC activates cadBA expression in a lysine-independent, but pH-dependent manner [11, 19]. As expected, in the lysP – background, CadC_C208A,C272A induced cadBA expression lysine- and pH-independently revealing that LysP is responsible for the inhibition Romidepsin clinical trial of CadC_C208A,C272A in the absence of lysine at pH 7.6 (data not shown). As discussed below, these experiments revealed that CadC without a disulfide bond is transformed into a semi-active state with respect to both the pH and the lysine

stimuli. Periplasmic disulfide oxidoreductases have no major influence on CadC activation The results described above led to the hypothesis that at physiological pH CadC contains a disulfide bond which is reduced at low pH. Opening and formation of disulfide bonds requires either the corresponding environment (oxidizing or reducing) or enzymes that catalyze these processes. Therefore, we analyzed whether periplasmic proteins known to be involved in formation and opening of disulfide Napabucasin mouse bonds during the protein folding process such as the Dsb proteins [20] have an influence on CadC activation. Six gene deletion mutants were constructed lacking the disulfide bond-modifying proteins DsbA, DsbB, DsbC, DsbD, DsbG and CcmG (also known

as DsbE). CcmG does not belong to the Dsb system, but is a membrane-anchored protein with a periplasmic thiol:disulfide oxidoreductase domain involved in cytochrome c biogenesis [21]. DsbA is a disulfide oxidase responsible for the formation of disulfide bonds and is recycled by the membrane protein DsbB [20]. DsbC is an isomerase that opens wrongly formed disulfide bonds and introduces the correct ones and as such also exhibits a reductase activity. DsbG is a non-essential isomerase that is able to substitute

for DsbC, and seems to protect single cysteines from oxidation that are needed in a reduced state to be catalytically active [22]. Both, DsbC and DsbG, are recycled by DsbD. While DsbB and DsbD are membrane proteins, DsbA, DsbC and DsbG are soluble proteins located in the periplasm. Mutants of E. coli MG1655 each lacking a single dsb Ribonucleotide reductase gene were grown at pH 5.8 and 7.6 in the presence of external lysine, and lysine decarboxylase (CadA) activity was determined as a measurement for the expression level of cadBA and thus of the functionality of CadC (Figure 6). All strains tested exhibited a pH-dependent regulation that was comparable to the wild-type strain, though the fold-induction differed slightly in some mutants. Under inducing conditions (pH 5.8, lysine) CadA activity was more than twice as high in the mutant MG1655ΔdsbA, lacking the disulfide oxidase DsbA, as in the wild-type strain MG1655 [specific CadA activity of 2.96 μmol/(min*mg protein) instead of 1.27].

The data are shown in a dose-dependent Cytoskeletal Signaling inhibitor manner. Figure 3 Effects of recombinant human Mullerian-inhibiting substance (MIS)/anti-Mullerian hormone (E.Coli derived) on endometriosis stromal cell line. (A) pre-G1 fraction analysis of endometriosis stromal cells treated for 24-48-72 hrs with the indicated final concentrations of MIS. The data are shown in a time-dependent manner. (B) pre-G1 fraction analysis of endometriosis stromal cell line treated for 24-48-72 hrs with the indicated final concentrations of MIS. The data are shown in a dose-dependent manner. (C) Cell

cycle analysis of endometriosis stromal cells treated for 24-48-72 hrs with the indicated final concentrations of MIS. The data are shown in a time-dependent manner. (D) Cell cycle analysis of endometriosis stromal cells treated for 24-48-72 hrs with the indicated final concentrations

of MIS. The data are shown in a dose-dependent manner. Figure 4 Effects of purified recombinant protein of Homo Sapiens anti-Mullerian hormone (AMH) on endometriosis stromal cell line. (A) Cell cycle analysis of endometriosis stromal cells treated for 48 hrs with AMH at 1000 ng/mL. Proteasome inhibition assay (B) pre-G1 fraction analysis of endometriosis stromal cells treated for 48 hrs with AMH at 1000 ng/mL. Figure 5 Analysis of AMH, AMHRII expression and CytP450 activity. (A) Real-time PCR to assess the percentage of expression levels of AMH (1), AMH (2), AMH type II Receptor (1) and (2) (AMH RII) genes in endometrial epithelial and stromal cell line respectively. (B) Expression levels of the Cytochrome P4501 and 2 isoforms and Reverse Transcriptase–Polymerase Chain Reaction (RT-PCR) for the CytP (450) 1 and 2 in epithelial and stromal cell line respectively; GAPDH represents loading control. (C) CYP Activity assay in endometrial stromal cells treated for 24 hrs at 1000 ng/mL of MIS

full-length. (D) CYP Amylase Activity assay in endometrial stromal cells treated for 24 hrs at 1000 ng/mL of Plasmin-cleaved MIS. Considering that the plasmin-digested AMH has been reported to be more active in cultured human endometrial cell lines [15], human plasmin was used to cleave and activate the recombinant Human AMH at its monobasic arginine-serine site at residues 427-428 and then tested in functional experiments on both endometriosis stromal and epithelial cells. Firstly, we found that plasmin-digested AMH can alter the expression or function of CYP19, evaluated by testing CYP19 activity. The results suggest that the plasmin-digested AMH was able to suppress most of the CYP19 activity. When the plasmin-digested AMH was used on both endometriosis stromal and epithelial cells (Figure  6), an increase of pre-G1 phase treating with plasmin-digested AMH in both cell lines was detected, most marked in the epithelial cells (Figure  6). Also the effect on induction of apoptosis was stronger during the first 24 hours of treatment (Figure  6A-B).

Nat Meth 2008, 5:235–237.CrossRef 27. Huse SM, Dethlefsen

L, Huber JA, Welch DM, Relman DA, Sogin ML: Exploring microbial diversity and taxonomy using SSU rRNA hypervariable tag sequencing. PLoS Genet 2008,4(11):e1000255.PubMedCrossRef Authors’ contributions JYW participated in the design of the study and performed the molecular experiments, XTJ participated in the bioinformatics analysis, SYL participated in the molecular experiments, FZ participated in the design of the study, HWZ participated in the design of the study, analyze the data and draft the manuscript. All authors read and approved the final manuscript.”
“Background Polyhydroxyalkanoates (PHA) are intracellular carbon storage polyesters that are produced by a wide variety of bacteria [1]. The most common PHA variants are so-called short chain length (scl-) PHAs Selleckchem ALK inhibitor containing monomers with 4 and/or 5 carbon-atoms [1]. Most other PHAs are referred to as medium chain length (mcl-) PHAs because the monomers generally consist of 3-hydroxyalkanoic acids with 6 or

more C-atoms [2]. These mcl-PHAs which are produced by fluorescent pseudomonads have application potential as elastomeric biodegradable plastics [3] or as sources of chiral monomers [4–6]. Pseudomonas putida accumulates mcl-PHA in discrete granules covered by a phospholipid monolayer in which various proteins are embedded [7, 8]. These granule-associated proteins include PHA polymerases (PhaC), PHA depolymerase (PhaZ) [9–11], CYC202 nmr phasins (PhaF and PhaI) [7, 12, 13] and acyl-CoA synthetase [14]. PHA polymerases (also referred to as PHA synthases), which use CoA-activated 3-hydroxy

fatty acids as substrates, are the key enzymes in mcl-PHA biosynthesis [15]. In P. putida U, two PHA polymerases encoded by phaC1 and phaC2 are known MycoClean Mycoplasma Removal Kit [16]. Disruption of phaC2 appeared to reduce the accumulation of PHA by two thirds, whereas disruption of phaC1 resulted in a complete loss of PHA accumulation [16]. Intracellular mcl-PHA degradation proceeds through the action of a PHA depolymerase encoded by phaZ. The enzyme has been suggested to act via an exo-acting hydrolytic mechanism [17]. The major amount of granule associated proteins in P. putida is accounted for by the phasins PhaI and PhaF [12, 13]. These amphiphilic proteins undoubtedly have a structural role in the granule, by which a barrier is created between the hydrophobic surface of the polymer and the surrounding hydrophilic cytoplasm [18]. In addition, PhaF may also regulate PHA metabolism at the transcriptional level [13]. Little is known of how mcl-PHA accumulation and degradation are controlled in pseudomonads. Previous studies have demonstrated that in P. putida, PHA polymerases and PHA depolymerase are concomitantly active, resulting in parallel synthesis and degradation [19].

Index Herbariorum: A global directory of public herbaria and associated staff. New York Botanical Garden’s Virtual Herbarium. http://​sweetgum.​nybg.​org/​ih/​] Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876–4882CrossRefPubMed Vellinga EC (2001) Macrolepiota. In: Noordeloos

ME, Kuyper TW, Vellinga EC (eds) Flora Agaricina Neerlandica, vol. 5. A. A. Balkema Publishers, Lisse (Netherlands) Vellinga EC (2003) Chlorophyllum and Macrolepiota (Agaricaceae) in Australia. Austr Syst Bot 16:361–370CrossRef Vellinga EC, Yang ZL (2003) Volvolepiota and Macrolepiota—Macrolepiota velosa, a new species from

China. Mycotaxon selleckchem 85:183–186 Vellinga EC, De Kok RPJ, Bruns TD (2003) Phylogeny and taxonomy of Macrolepiota (Agaricaceae). Mycologia 95(3):442–456CrossRef Wasser SP (1993) Tribes Cystodermateae Sing. and Leucocoprineae Sing. of the CIS and Baltic States. Libri botanici 9. Eching: IHW-Verlag White TJ, Bruns T, Lee S, Taylor J (1990) Amplification and direct sequencing of fungal ribosomal RNA genes for phylogenies. In: Innis MA, Gelfand DH, Sninsky JJ, White TJ (eds) PCR protocols: a guide to methods and applications. Alvelestat mw Academic Press, San Diego, pp 315–322 Yang ZL (2000) Type studies on agarics described by N. Patouillard (and his co-authors) from Vietnam. Mycotaxon 75:431–476 Ying JZ, Zang M (eds.) (1994) Economic macrofungi from southwestern China. Beijing: Science Press.

399 pp. (in Chinese) Ying JZ, Wen HA, Zong YC (1994) The Economic macromycetes from western Sichuan. Science, Beijing, in Chinese Yuan MS, Sun PQ (2007) Atlas of Chinese mushrooms. Sichuan Publishing House of Science and Technology, Chengdu, p 552, in Chinese Zang M, Li B, Xi JX (1996) Fungi of Hengduan mountains. Science, Beijing, in Chinese”
“Introduction Fungi play a central role in most ecosystems and seem to dominate the microbial biomass in soil habitats (Joergensen and Wichern 2008), where they are important decomposers and occupy a notable position in the natural carbon, nitrogen and phosphorus Rho cycles (Christensen 1989). Mycorrhizal and parasitic communities in different habitats are well characterised at the molecular level (Ryberg et al. 2009), and they directly affect plant community composition and productivity (Klironomos 2002; van der Heijden et al. 2008). In contrast, fungal species inventories from agricultural soils are so far mainly known from cultivation studies (Domsch and Gams 1970; Domsch et al. 1993; Hagn et al. 2003), while there are only few studies employing cultivation-independent techniques (de Castro et al. 2008; Lynch and Thorn 2006). A solid knowledge of the fungal community in agricultural soils provides the basis for functional studies about specific processes carried out by members of this group.

Authors’ contributions PP, study conception and design, data acquisition, manuscript drafting. MB, manuscript drafting, methodological advise. MC, critical revision for important intellectual contents. MDM, critical revisions for important intellectual contents. AS, critical revisions for important intellectual contents. MD, critical revisions for important intellectual contents. AF, critical revisions for important intellectual contents. AL, critical revisions for important intellectual contents. FP, critical revisions for important intellectual contents. PM, critical revisions for important intellectual contents. GC, critical revisions

for important intellectual contents; AA, critical revisions for important intellectual contents. CN, critical revisions for important intellectual contents. AD, critical revisions for important intellectual contents. GDT, data analysis, AZD1208 mw results’ interpretation. MLB, critical revisions for important intellectual contents. AM, critical revisions for important intellectual contents. IRM, Tanespimycin data acquisition, methodological advise. AG, study conception and design, methodological advice. All authors read and approved the final manuscript.”
“Background

The Na+/K+ ATPase catalyzes the electrogenic exchange of three intracellular Na+ ions for two extracellular K+ ions using for this transport energy that is released from the hydrolysis of ATP. In this way Na+/K+ ATPase plays an important role in the regulation of intracellular Na+ and K+ concentrations and in the maintenance of electrical membrane potential, cell volume, and Na+-coupled transport of amino acids, glucose, nucleotides, and other compounds with low molecular mass [1–3]. Ouabain (OUA) is a cardiac glycoside that has been used for long time for the treatment of cardiac insufficiency. OUA by binding to the α-subunit of Na+/K+ ATPase inhibits 17-DMAG (Alvespimycin) HCl it. The inhibition of the Na+/K+ ATPase, reducing the sodium gradient, leads to increased cytosolic [Ca++ probably by impairing the activity of the Na+/Ca++-exchanger (NCX)

[4–9]. NCX is one of the main pathways for intracellular Ca++ clearance [9] and the inhibition of the Na+/K+ ATPase by cardiac glycosides, causing the inversion of the Na+/K+ gradient, leads to impairment of the NCX activity, contributing to accumulation of Ca++[4–9]. Results from epidemiological studies showed significantly lower mortality rates in cancer patients receiving cardiac glycosides, which turned on interest in the antineoplastic properties of these drugs [10]. In various cancer cell lines, including prostate cancer cells or breast tumor cells, cardiac glycosides induce apoptosis [11–16]. These glycosides are considered to be cytotoxic for tumors because malignant cells express high levels of Na+/K+ ATPase α-isoforms, which are inhibited by them [17].

Additional polysaccharides were removed following the protocol outlined in Wilson [27]. FS ATCC43239 gDNA was isolated following the protocol described in Ausubel et al. [28] and FA UTEX1903 gDNA was extracted following a protocol described in https://www.selleckchem.com/products/abt-199.html Mustafa [29]. Whole genome sequencing and bioinformatics High molecular weight gDNA from WI HT-29-1 and HW IC-52-3 was sent to BGI (Beijing Genome Institute, China) for genome sequencing via high throughput Illumina sequencing technology. BGI performed genome assembly and gene annotation using Glimmer v3.0. Extracted gDNA from FA UTEX1903 and FS ATCC43239 was submitted to Case Western Reserve Genomics Core Facility for whole genome sequencing. Paired end

DNA libraries were obtained by using Nextera DNA sample preparation kit and sequenced using the Illumina GAIIx platform. Raw reads quality was assessed using FastQC 0.10.1 (Babraham Bioinformatics) with default settings AUY-922 price and trimmed with Seqyclean 1.3.12 (http://​cores.​ibest.​uidaho.​edu/​software/​seqyclean). Filtered

reads were assembled de novo using the velvet package (Version 1.2.08) and a kmer range between 55-63. The optimal assembly based on expected genome size, N50 and contig number was used for downstream annotation and analysis. Gene annotation was performed by BGI using Glimmer v3.2. A Basic Local Alignment Search Tool (BLAST) search was performed to identify the putative function of proteins based on sequence similarity [30]. Nucleotide and protein sequences were organized and visualized using Sucrase Geneious v6.1.7 created by Biomatters. Available from http://​www.​geneious.​com/​. Nucleotide alignments were performed using Geneious Alignment with default settings. For protein alignments, Clustal Omega (Version 1.2.1) was used with default settings, except order changed from aligned to input [18]. For phylogenetic analysis, the sequences were first aligned using the Clustal W program built into Geneious. Phylogenetic trees were constructed using the Geneious Tree Builder program, which uses the neighbour-joining method [31]. A 929 bp nucleotide fragment was

used for the phylogenetic analysis of 16S rDNA sequences, while a 315 amino acid sequence alignment was used for phylogenetic analysis of the prenyltransferase. The outgroup was constituted by the distantly related cyanobacterium Synechocystis sp. for 16S rDNA analysis. PCR and sequencing reactions A 50 μL PCR reaction mixture contained 10 pmol of specific forward and reverse primer (Additional file 11) (Geneworks, Australia), 1× PCR Buffer (KAPA Biosystems), 2.5 mM MgCl2, 1 pmol dNTPs (Fisher Biotec), 1 U of KapaTaq polymerase (KAPA Biosystems) and 50 ng of gDNA template. Pfu DNA polymerase (Sigma) was used in addition to KapaTaq at a ratio of 1:10 (v/v). Hotstart PCR was performed by first heating the samples to 95°C.

Authors’ contributions ZDM wrote the paper and prepared the samples. LZ, SY, QS, and KU analyzed the sample. KYC performed the TEM. WCO coordinated the study as the corresponding author. All authors read and approved the final manuscript.”
“Correction In the Methods section of our published article [1],

the evolution of grain size and microstrain in the Mg and Cu is estimated using the single-line method of diffraction line-broadening analysis. However, a very important reference is omitted, and this method founder’s publication should be cited here [2]. selleck Moreover, the experimental results contained in this paper were obtained by the first author in cooperation with Dr. U. Welzel, Dr. E. Bischoff and Prof. Dr. E.J. Mittemeijer (all Max Planck Institute for Intelligent selleck screening library Systems) during the stay of the first author in the department of Prof. Dr. Mittemeijer. Thus the authors would like to express our gratitude to them in the Acknowledgements section of this published article [1]. References 1. Ma ZQ, Liu YC, Yu LM, Cai Q: Investigation of phase composition and nanoscale microstructure of high-energy ball-milled MgCu sample.

Nanoscale Res Lett 2012, 7:390.CrossRef 2. de Keijser TH, Langford JI, Mittemeijer EJ, Vogels ABP: Use of the Voigt function in a single-line method for the analysis of X-ray diffraction line broadening. J Appl Cryst 1982, 15:308–314.CrossRef”
“Background Ultraviolet (UV) photodetector has been a popular Doxorubicin research issue for its potential applications in a wide range of fields, such as remote control, chemical analysis, water purification, flame detection, early missile plume detection, and secure space-to-space communications [1]. To avoid the use of filters and achieve visible-blind

operation, wide bandgap semiconductors, such as GaN, SiC, ZnO, and TiO2[2–8], have been studied during the last decade for wide-spreading usage in photodetection, especially in the ultraviolet region. Among conventional available UV photodetectors, quite many kinds of structures have been fabricated, which in most cases are based on epitaxial growth process and various solid-state junction structures. Typical examples are photodetectors based on p-n junction, p-i-n photodiodes, Schottky barrier (SB), metal–semiconductor-metal, and metal-insulator-semiconductor structures [9–15]. These photodetectors typically require an external bias as the driving force to prevent the recombination of photogenerated electron–hole pairs. For large-area two-dimensional arrays that contain huge amounts of small UV sensors, energy supply will be one of the main challenges for such sensor systems. Recently, self-powered nanodevices and nanosystems have attracted lots of attention due to their various advantages. Xu et al.

Co-registration Periosteal and endosteal bone surfaces of the QCT datasets were segmented using the Medical Image Analysis Framework software package developed at the University of Erlangen [17]. A tetrahedral mesh model with third-order Bernstein Palbociclib manufacturer polynomial density functions was then calculated from the segmented QCT volume [18, 19]. The meshed QCT

volume was co-registered to the four DXA images using a general purpose 2D–3D deformable body registration algorithm [20–23]. A rigid registration allowing rotations and translations but not deformations was used. The 2D–3D registration algorithm used a fast GPU-based algorithm [24] to produce digitally reconstructed fan beam radiographic projections (DRRs) of the meshed volume at each angle that a DXA image was obtained. Each of the four DRRs was compared to the corresponding DXA image using mutual information. The sum of the mutual information of these image pairs served as a cost function. An optimization routine using simulated annealing (a robust method that avoids being trapped in local minima [25]) was used to determine the correct transform for the three translational and rotational parameters of the QCT meshed volume to co-register MAPK Inhibitor Library purchase it with the DXA images. The inverse of this transform was used to place a 1 mm plane at the center of the HSA NN and IT ROIs (which were defined

on the standard hip PA DXA image), onto the QCT dataset. This plane is the 2D slice on which the QCT parameters are calculated. The procedure of co-registration ensured that anatomically equivalent regions were measured by HSA and QCT. Because many of the QCT scans did not extend far enough below the lesser trochanter into the femoral shaft to allow a comparison to the HSA shaft ROI,

the comparison at the shaft ROI was not attempted. Calculation of parameters on the QCT dataset Cross-sectional area (CSA) in square centimeters was defined in accordance with the traditional GPX6 HSA definition as the area of the slice filled with bone. In this definition, the area of each pixel is weighted by the amount of bone in the pixel. Cross-sectional moment of inertia (CSMI) in quartic centimeters is defined around a given axis. In DXA HSA, CSMI is calculated and averaged over line profiles along the u direction in Fig. 1. The center line profile of HSA is a projection of the 2D slice in the PA image. CSMIHSA can therefore only be calculated around an axis perpendicular to the PA image (v in Fig. 1). However, QCT is not restricted by the directionality of the PA image, and one is free to choose the axis around which CSMI is calculated. Let (u, v, w) define an ortho-normal coordinate system centered at the center of mass (COM) of the 2D slice, ρ(u, v) be the volumetric bone density in milligrams per cubic centimeter per voxel in the slice, and ρ NIST = 1,850 mg/cm3.

The entire process was repeated with the frozen stock serving as the seed for the inoculum. Figure 5 Enrichment of pools with enhanced invasion into CT-26 cells. Glycerol stocks from the L. lactis banks (both pre and post enrichment passages-including controls: InlAWT and InlA m * expressing L. lactis) were incoulated into GM17 media. Nisin induced cultures were invaded into CT-26 monolayers. Invasion was expressed relative to L. lactis InlAWT (set as

100 percent). The graph is of the data from one experiment. Table 2 Supplementary information for Figure 6. Clone 1 2 3 4 5 6 7 8 (iii) Low T273I Q190L Q190L Q190L Q190L T229P G303E Q190L Q190L N386I Fold increase vs Wt 9.44 5.82 6.98 4.15 13.23 12.12 6.10 7.94 (iv) Medium T164A K301I G303E T399I L86F N143K P159A Q196L K218M V224A ABT-263 solubility dmso G303E Q306H Q190L L329Q S470C T164A K301I G303E N259Y T399I Q190L G248R F193Y K301E N413Y K507I T164A K301I G303E Fold increase vs Wt 3.25 9.31 7.79 6.85 8.14 6.57 4.05 10.08 (v) High L149M N259Y Q190L S223C N252Y I351T S173I G303E T446A D449H S173I T268I G303E T446A D449H Q190L S223C N252Y I351T N259Y N239D S311C N325D S173I L185F L188I Fold increase vs Wt 23.21 15.89 8.64 Selleck Cilomilast 19.31 9.08 16.36 8.24 15.42 (vi) Very High

Q190L A270G K301G V123A Q190L P290Q N349D Q190L Q196K P290S L404S N413Y D457V N130I F150V L203F Y369F N381I S487N L294V S308R Y369S N381I S487N L122I S292T E330V I458V Q190L D199V S377N P444S K495N Fold increase vs Wt 4.14 9.33 6.96 8.71 9.56 7.12 7.51 9.33 Mutations identified in the BglII/BstXI fragment of pNZBinlA (iii-vi) and the invasion increase into CT-26 cells versus L. lactis

InlAWT. The amino acid mutations identified which involved in the interaction between InlAWT and hCDH1 are highlighted in bold. Details highlighted in bold and italics are mutations recombined in the chromosome of EGD-e. L. lactis Buspirone HCl InlA site directed mutants with fold invasion increase into CT-26 cells vs L. lactis InlAWT in brackets: S192N (21), Y369 S (20), S192N+Y369 S (30). Below: Amino acids in InlAWT which interact with hCDH1 and amino acid changes identified from error prone PCR screen. R85, N104: D Q*, N107, F150: V, E170, E172: T*, Q190: L, S192, R211, D213, I235, T237, E255, N259: Y, K301: I E G, N321: Y, E323, N325: D, E326, Y343, T345, Y347, F348, R365, F367, Y369: F S, W387, S389. * N104 and E172 mutations were found from additional screens and sequencing. Figure 6 Invasion attributes of individual L. lactis clones post CT-26 enrichment (passage 6) into Caco-2 (grey bars) or CT-26 (white bars) cells. From each of the four banks, eight clones were picked and invaded with invasion expressed as the average (with standard deviation) from triplicate wells. Sequnce data of the clones is presented in Table 2. Letters above bars indicate sequences that were subsequently used to recreate into the L. monocytogenes chromosome.

The alignments were done using MUSCLE [46]. Acknowledgements The work was financed by Colciencias (project No. 657045921709). We would like to thank J.M. Anzola, D. Riaño, J. Rodríguez and D. Chaves for discussions and help with the bioinformatics analysis. Electronic supplementary material Additional file 1: Title:

Inventory of GGDEF proteins in K. pneumoniae 342, MGH 78578 and NTUH-K2044. (PDF 235 KB) Additional U0126 mouse file 2: Title: Inventory of EAL proteins in K. pneumoniae 342, MGH 78578 and NTUH-K2044. (PDF 202 KB) References 1. Hoyos-Orrego SR-RO, Hoyos-Posada C, Mesa-Restrepo C, Alfaro-Velásquez M: Características clínicas, epidemiológicas y de susceptibilidad a los antibióticos en casos de bacteriemia por Klebsiella pneumoniae en neonatos. AZD2014 Rev CES Med 2007,21(2):31–39. 2. Struve C, Krogfelt KA: Pathogenic potential of environmental Klebsiella pneumoniae isolates. Environ Microbiol 2004,6(6):584–590.PubMedCrossRef 3. Podschun R, Ullmann U: Klebsiella spp. as nosocomial pathogens: epidemiology, taxonomy, typing methods, and pathogenicity factors. Clin Microbiol Rev 1998,11(4):589–603.PubMed 4. Yu VL, Hansen DS, Ko WC, Sagnimeni A, Klugman KP, von Gottberg A, Goossens H, Wagener MM, Benedi VJ: Virulence characteristics of Klebsiella and clinical manifestations of K.

pneumoniae bloodstream infections. Emerg Infect Dis 2007,13(7):986–993.PubMedCrossRef 5. Marschall J, Fraser VJ, Doherty J, Warren DK: Between community and hospital: healthcare-associated gram-negative bacteremia among hospitalized patients. Infect Control Hosp Epidemiol 2009,30(11):1050–1056.PubMedCrossRef 6. Fouts DE, Tyler HL, DeBoy RT, Daugherty S, Ren Q, Badger JH, Durkin AS, Huot H, Shrivastava S, Kothari S, et al.: Complete genome sequence of the N2-fixing broad host range endophyte Klebsiella pneumoniae 342 Leukocyte receptor tyrosine kinase and virulence predictions verified in mice. PLoS Genet 2008,4(7):e1000141.PubMedCrossRef 7. Balestrino D, Ghigo JM, Charbonnel N, Haagensen JA, Forestier C: The characterization of functions involved in the establishment and maturation of Klebsiella pneumoniae in vitro biofilm reveals dual roles for surface exopolysaccharides. Environ Microbiol 2008,10(3):685–701.PubMedCrossRef

8. Boddicker JD, Anderson RA, Jagnow J, Clegg S: Signature-tagged mutagenesis of Klebsiella pneumoniae to identify genes that influence biofilm formation on extracellular matrix material. Infect Immun 2006,74(8):4590–4597.PubMedCrossRef 9. Balestrino D, Haagensen JA, Rich C, Forestier C: Characterization of type 2 quorum sensing in Klebsiella pneumoniae and relationship with biofilm formation. J Bacteriol 2005,187(8):2870–2880.PubMedCrossRef 10. Di Martino P, Cafferini N, Joly B, Darfeuille-Michaud A: Klebsiella pneumoniae type 3 pili facilitate adherence and biofilm formation on abiotic surfaces. Res Microbiol 2003,154(1):9–16.PubMedCrossRef 11. Johnson JG, Clegg S: Role of MrkJ, a phosphodiesterase, in type 3 fimbrial expression and biofilm formation in Klebsiella pneumoniae.