Plasmid pET30a was used as expression vector in E. coli BL21 (DE3). Escherichia coli–Bacillus shuttle vector pKSV7 (Smith & Youngman, 1992), which has a Bacillus temperature-sensitive

(ts) origin of replication, was used for gene replacement via homologous recombination at a nonpermissive temperature (30 °C) Chromosomal DNA of B. thuringiensis was isolated as described by Sambrook et al. (1989). PCR was performed with Pfu DNA polymerase (TaKaRa BioInc.) using the chromosomal DNA of B. thuringiensis as a template. The primers were designed according to the conserved region of the related proteins to clone the calY gene and its flanking sequences (Fig. 1a). The calY gene fragment was analyzed by 1% agarose gel LY2835219 supplier electrophoresis, purified, and cloned into pET30a check details vector according to the manufacturer’s instructions. The resultant plasmid was sequenced completely (Invitrogen, Shanghai, China) and designated pETCA. Escherichia coli transformation was carried out according to the method of Sambrook et al. (1989). Bacillus thuringiensis transformation was performed by electroporation in a Bio-Rad Gene Pulser Apparatus (Bio-Rad Ltd, Richmond, CA) according to the methods of Hu et al. (2009) and Xia et al. (2009). The plasmid pETCA was transformed

into E. coli BL21 (DE3). The overnight culture was diluted 100 times with fresh LB medium supplemented with 100 μg mL−1 kanamycin and incubated at 37 °C with shaking until the OD600 nm reached 0.6. Camelysin expression was then induced by adding isopropyl β-d-1-thiogalactopyranoside to a final concentration of 1 mmol L−1 and incubation for a further 4 h. The induced camelysin protein was purified by affinity

chromatography according to the protocol of HisTrap FF crude 1-mL column (GE Healthcare, Milwaukee, WI) and then used for antiserum production in rabbits as described previously (Chen et al., 2002). The E. coli–B. subtilis shuttle vector (pKSV7) which contained a temperature-sensitive B. subtilis Urease origin of replication (Smith & Youngman, 1992) was used to construct a calY replacement mutant. The general method is outlined in Fig. 1b. A 780-bp upstream fragment of gene calY was amplified with primer pair P7/P8 (Table 2). Its PCR fragment was digested with HindIII/SalI and cloned into the corresponding site of pUE containing an erythromycin-resistant cassette (erm) to generate pUES. An 800-bp downstream fragment was amplified with primer pair P9/P10 (Table 2). Its PCR fragment was digested with BamHI/EcoRI and cloned into the pUES to generate pUESX. A 2.8-kb HindIII/EcoRI fragment containing upstream and downstream fragments, erm was ligated into the corresponding site of pKSV7 to generate pKESX. The properties of pKESX that allow it to be used as a B. thuringiensis integration vector are as follows: (1) pKESX replicates in E. coli and B.

Conclusions. The most

common pathogens causing TD in Nepal were Campylobacter, ETEC, and Shigella. Because resistance to fluoroquinolone or azithromycin was similar, one of these drugs could be used as empiric therapy for TD with the other reserved for treatment failures. Diarrhea remains the most common illness among visitors and foreign residents in Kathmandu and travelers overall.1–5 In an exit poll at the Kathmandu airport, 68% of visitors experienced diarrhea in Nepal.3 The risk of diarrhea among expatriates in Nepal persists at a monthly rate of 27%.6 In a multicenter study reporting rate ratios for gastrointestinal infection after international travel, Nepal had the highest risk among 28 countries around the world.7 There are no published reports on antibiotic susceptibility for travelers’ diarrhea (TD) in Nepal. Clinical decisions based on microbiologic data from past LBH589 molecular weight research3,5 and data from other countries in the region8 may not be accurate, necessitating updated investigations. A joint project by the Canadian International Water and Energy Consultants (CIWEC) clinic and the Armed Forces Research Institute of Medical Sciences

(AFRIMS) in Bangkok was initiated in response to anecdotal reports of fluoroquinolone (FQ) failures among diarrheal cases seen by CIWEC practitioners in the late 1990s. The purpose of the initiative was to redefine the etiology of diarrhea in travelers and expatriates, to characterize antibiotic susceptibility Etofibrate patterns of microbiologic isolates and to A-769662 datasheet make comparisons with prior published data.3,5 Following approvals by the Nepal Health Research Council (FWA# 00000957) and the Human Use Research Committee, Walter Reed Army Institute of Research (FWA# 00000015), a case-control study was conducted with written informed consent from March 15, 2001, to March 15, 2003, at the CIWEC clinic. Persons studied were over age 18 years from high socioeconomic countries (United States, Western Europe, Japan, Australia, and New Zealand). Cases were those who reported at least three unformed stools in the preceding 24 hours and with

a stool specimen that conformed to the shape of the container. To provide a seasonal sampling over the 2 years of enrollment, the first two patients of the day who fulfilled these criteria were recruited. Controls were individuals seen at CIWEC during the same time period for complaints other than diarrhea who denied having diarrhea in the preceding 2 weeks and were willing to provide a stool sample. Cases and controls were not matched for age, gender, nationality, or duration of time in Nepal, so we could investigate these factors. All enrollees completed a standardized questionnaire detailing demographic and clinical factors, antibiotic use, recent travel history, and duration of time in Nepal. Cases were asked subjective questions characterizing the diarrhea. Enrollees were categorized as tourists or residents.

Therefore, lyophilized spores were mixed with a matrix solution containing either α-cyano-4-hydroxycinnamic acid [10 mg mL−1 in 50% acetonitrile/0.1% trifluoroacetic acid (TFA)] or sinapinic acid (20 mg mL−1 in 40% acetonitrile/0.1% TFA). These mixtures were spotted for analysis with a Shimadzu Biotech MALDI-TOF Mass Spectrometer (Axima Performance). Spectra of spores isolated from complex R5 medium (Kieser et al., 2000) or complex MS medium (Kieser

et al., 2000) showed peaks ranging from 1 to 12 kDa (Fig. 1a). Relative high intensities were observed for peaks with masses of 5070, 5121, 5182, and 5274 Da (Fig. 1b), which fit the predicted masses of ChpD, ChpH, ChpF, and ChpE, respectively (Claessen et al., 2003; Elliot p38 MAPK assay et al., 2003). Analysis of spores of the S. coelicolor chpABCDH (Claessen et al., 2003), chpABCDEH (Claessen et al., 2003), and chpABCDEFGH (Claessen et al., 2004) strains (obtained after prolonged incubation on MS medium) confirmed

the identity of these peaks, as they were absent in the respective mutants (Supporting Information, Fig. S1a). The rodlin proteins RdlA and RdlB (Claessen et al., 2002, 2004) were also identified at the spore surface as proteins with masses of 10 517 and 10 708 Da, respectively (Fig. S1b). NepA, whose presence on the spore surface has been demonstrated by immuno labeling (de Jong et al., 2009), could not be identified according to its predicted mass of 7725 Da. In contrast, SapB was found on the spore surface represented by a peak at 2027 Da. Interestingly, SapB was not only found on spores obtained from R5 medium (Fig. 1c) but Transferase inhibitor also on those obtained from MS medium (Fig. 1d), a condition in which Diflunisal SapB was formerly shown not to be secreted by the wild-type strain (Capstick et al., 2007). The intensity of the SapB peak on MS medium was about fourfold lower compared to that found with spores from R5 medium. SapB was also identified on spores on defined minimal medium with mannitol as a carbon source (Fig. 1e). Also in this medium, SapB is not secreted into the medium (Willey et al., 1991).

As expected, SapB was absent on spores of the ramR (Fig. S1c) and ramS mutants (Fig. 1c–e) that had been collected from cultures grown on R5 or minimal mannitol medium. Similar results were obtained when TFA extracts of spores were analyzed by MALDI-TOF MS (data not shown). The fact that SapB is not secreted in certain media (Willey et al., 1991; Capstick et al., 2007) suggested a difference between SapB secretion by vegetative hyphae and aerial hyphae and spores. To confirm this, culture media were analyzed for the presence of SapB by MALDI-TOF MS. Agar plates overlaid with cellophane disks were inoculated with spores of the wild-type strain or the ramR or ramS mutant strains. After 5 days of growth at 30 °C, the agar medium underlying the cellophane membrane was collected and melted.

There were no significant

differences in terms of the LPV fu% (P=0.234). One patient (9%) in the first/second trimester selleck compound library and eight patients (19%) in the third trimester had undetectable (<5 ng/mL) unbound LPV concentrations (undetectable=excluded). However, the majority of these individuals had correspondingly low (<1000 ng/mL) total LPV levels. In a paired analysis of 12 patients with matched second/third trimester and postpartum samples, geometric mean total LPV concentrations were significantly (∼29%) reduced antepartum compared with postpartum (P=0.021) (Table 3), as were total RTV plasma concentrations. These patients also had measurements taken in the first (n=3) and/or second R428 (n=5) trimesters, respectively, as shown in Figure 1. One patient had a missing third trimester value as she delivered prematurely

(at 27 weeks), and therefore her TDM in the second trimester (22 weeks) was compared with her postpartum TDM. Nine of the 12 patients (75%) experienced an increase in LPV Ctrough postpartum (Fig. 1). Of the three patients with a decreased LPV Ctrough postpartum, one had previously received an LPV/r dose increase in the third trimester but reverted back to two tablets twice daily post-delivery. The remaining two patients had suspected compliance issues. One patient reported missing her night-time dose approximately once a week and the other had a history of noncompliance (she had been noncompliant in a previous pregnancy and had delivered an HIV-positive child), but in this study her records stated that she was fully compliant. The timing of pharmacokinetic sampling in these patients (both time post-dose and weeks postpartum) was consistent with that of other study participants. There were no significant differences in absolute LPV unbound Bumetanide concentrations (P=0.081) and fu% (P=0.537) at the third trimester vs. postpartum. In the present study, LPV (total and unbound) trough concentrations were determined sequentially during

pregnancy and at postpartum in women receiving the LPV/r tablet formulation at standard (400/100 mg twice daily) dosing. We observed that total LPV and RTV trough concentrations [geometric mean (95% CI)] were reduced in the third (and second) trimester(s) of pregnancy, in relation to corresponding concentrations postpartum. These data are consistent with previous reports on the LPV/r SGC (400/100 mg twice daily) in pregnancy. Furthermore, in a paired analysis of 12 patients, nine experienced an increase in LPV Ctrough at the time of postpartum sampling (Fig. 1), suggesting that plasma concentrations had normalized by approximately a median (range) of 8 (5–12) weeks postpartum. The clinical significance of decreased LPV concentrations during pregnancy is uncertain.

There were no significant

differences in terms of the LPV fu% (P=0.234). One patient (9%) in the first/second trimester this website and eight patients (19%) in the third trimester had undetectable (<5 ng/mL) unbound LPV concentrations (undetectable=excluded). However, the majority of these individuals had correspondingly low (<1000 ng/mL) total LPV levels. In a paired analysis of 12 patients with matched second/third trimester and postpartum samples, geometric mean total LPV concentrations were significantly (∼29%) reduced antepartum compared with postpartum (P=0.021) (Table 3), as were total RTV plasma concentrations. These patients also had measurements taken in the first (n=3) and/or second TAM Receptor inhibitor (n=5) trimesters, respectively, as shown in Figure 1. One patient had a missing third trimester value as she delivered prematurely

(at 27 weeks), and therefore her TDM in the second trimester (22 weeks) was compared with her postpartum TDM. Nine of the 12 patients (75%) experienced an increase in LPV Ctrough postpartum (Fig. 1). Of the three patients with a decreased LPV Ctrough postpartum, one had previously received an LPV/r dose increase in the third trimester but reverted back to two tablets twice daily post-delivery. The remaining two patients had suspected compliance issues. One patient reported missing her night-time dose approximately once a week and the other had a history of noncompliance (she had been noncompliant in a previous pregnancy and had delivered an HIV-positive child), but in this study her records stated that she was fully compliant. The timing of pharmacokinetic sampling in these patients (both time post-dose and weeks postpartum) was consistent with that of other study participants. There were no significant differences in absolute LPV unbound Rho concentrations (P=0.081) and fu% (P=0.537) at the third trimester vs. postpartum. In the present study, LPV (total and unbound) trough concentrations were determined sequentially during

pregnancy and at postpartum in women receiving the LPV/r tablet formulation at standard (400/100 mg twice daily) dosing. We observed that total LPV and RTV trough concentrations [geometric mean (95% CI)] were reduced in the third (and second) trimester(s) of pregnancy, in relation to corresponding concentrations postpartum. These data are consistent with previous reports on the LPV/r SGC (400/100 mg twice daily) in pregnancy. Furthermore, in a paired analysis of 12 patients, nine experienced an increase in LPV Ctrough at the time of postpartum sampling (Fig. 1), suggesting that plasma concentrations had normalized by approximately a median (range) of 8 (5–12) weeks postpartum. The clinical significance of decreased LPV concentrations during pregnancy is uncertain.

The vector pET4TH used for the synthesis of the recombinant 4THase without the signal peptide was described previously (Kanao et al., 2007). Escherichia coli BL21 Star™(DE3) harboring pET4TH was cultured in a modified Terrific broth medium [90 mM potassium phosphate buffer (pH 7.2) containing 1.2% w/v tryptone, 2.4% w/v yeast extract, and 0.4% v/v glycerol] supplemented with ampicillin (50 μg mL−1) at 37 °C to an OD660 nm of 1.0. Expression of the recombinant gene was induced by adding 1 mM isopropyl-β-d-thiogalactopyranoside (IPTG) to the culture, followed by incubation

at 20 °C for 36 h. Cells were harvested by centrifuging at 10 000 g for 10 min and washed three times with 100 mM of potassium phosphate buffer (KPB) (pH 7.0). The bacterial pellets were suspended in 100 mM KPB (pH 7.0) containing 2 mM dithiothreitol and disrupted by sonication on ice (the total ‘on’ period was 15 min in cycles of 30 s ‘on’ and 30 s ‘off’). The insoluble fraction BTK inhibitor molecular weight was collected by centrifugation at 10 000 g for 10 min, and the supernatant was removed. The pellet was washed three times with 10 mM Tris-HCl buffer (pH 8.0) containing 1 mM EDTA. In order to collect the inclusion bodies, the pellet was washed with 100 mM KPB (pH 7.0) containing 4% v/v Triton X-100 three times. The inclusion NSC 683864 bodies were washed again

three times with sterilized distilled water to remove the detergent. The standard refolding protocol was performed as follows: recombinant proteins from the inclusion bodies were solubilized with a 6 M guanidine hydrochloride solution containing 10 mM dithiothreitol and subsequently centrifuged at 10 000 g for 10 min. The supernatant (1 mL)

containing solubilized recombinant protein was dialyzed against the refolding buffer (100 mL) at 4 °C with gentle stirring for 1 h. A solution containing 4 M guanidine hydrochloride, 10 mM β-alanine, 30% v/v glycerol, 0.4 M ammonium sulfate, and 2 mM dithiothreitol was used as the initial refolding buffer. The pH was adjusted to 4.0 with sulfuric acid. After the 1-h dialysis, the concentration of guanidine hydrochloride Thymidylate synthase in the refolding buffer was gradually decreased by pumping the same buffer without guanidine hydrochloride into the refolding buffer using a peristaltic pump (90 s mL−1). When the volume of the refolding buffer reached 200 mL (the guanidine hydrochloride concentration was 2 M at this stage), 100 mL of the refolding buffer was removed. This dilution step was performed four times in total. When the concentration of guanidine hydrochloride in the refolding buffer was diluted to 0.25 M, the refolding buffer was replaced with a buffer (pH 4.0) containing 0.1 M β-alanine and 0.4 M ammonium sulfate. The recombinant protein solution (1 mL) was dialyzed against the buffer (1000 mL) for 3 h with gentle stirring at 4 °C. After dialysis, the dialyzed solution was centrifuged at 10 000 g for 10 min to remove insoluble proteins.

maltophilia R551-1 and selleck compound k279a is also low, that is below the ‘cut-off ’ for species delineation (Richter & Rossello-Mora, 2009). While many strains have been isolated and characterized as S. maltophilia, the other species in this genus have been more sparsely represented. In fact, all novel species of Stenotrophomonas described since 2006 have included descriptions only of single strains, which makes it impossible to assess comprehensive intraspecific variations. In this study, additional strains with identical or nearly identical 16S rRNA gene sequences to the respective type strains of four species have been included. The two S. nitritireducens strains included

in this study exhibited genomic DNA similarities of 78% to 85% and have identical 16S rRNA gene sequences (Finkmann et al., 2000). The gyrB Region 1 of these two strains was 99.0% similar. S. acidaminiphila strain CCUG 54933 had the identical 16S rRNA gene sequence as S. acidaminiphila CCUG 46877T. Their gyrB Region 1 sequences were observed to differ by 4.0%. The second strain of S. rhizophila, CCUG 47044, had the FG4592 identical 16S rRNA gene sequence to that of the type strain of the species, CCUG 54934T (Wolf et al., 2002). The gyrB Region 1 sequences

of these two strains were observed to be 98.6% similar. A clinical isolate, CCUG 56889, exhibited 99.9% 16S rRNA gene sequence similarity to that of the S. chelatiphaga type strain, CCUG 57178T. The gyrB Region 1 of these two strains were 95.4% similar (Fig. 2 and Table S2). In summary, the nucleotide sequences of many gyrB provide much greater resolution between the species in the Stenotrophomonas genus than the sequences of the more conserved 16S rRNA gene. This observation was expected for a protein-coding ‘housekeeping’ gene and is what has been observed for the gyrB gene sequences of other taxa. The sequences of Region 2 of gyrB exhibited greater variation than Region 1, although for the more

closely related species, as well as strains of a given species, the two different gyrB gene regions provided similar levels of separation. Several of the Stenotrophomonas spp. have been previously compared by MLSA including seven partial genes (not gyrB). In that study, interspecies similarities of the concatenated partial gene sequence were approximately 90–95% for the type strains of the validly described species included (Vasileuskaya-Schulz et al., 2011). The resulting clustering was similar to what is shown in this study. The levels of gyrB sequence similarity also correlated well with the genomic DNA similarity levels. All validly published and currently recognized species, except S. maltophilia/S. pavanii, were < 93% similar (for both sequenced regions). Strains of a given species were more than 95% similar. However, several strains within the ‘S. maltophilia complex’ were approaching and even exceeding this border (i.e. S. pavanii and the strain S. maltophilia R551-3).

The mlrA of EMS may have been obtained from one or more of

the Sphingopyxis species. Microcystin-degrading bacteria, which possess mlr genes, may play an important role in decreasing microcystin in Lake Taihu and other water bodies. Because mlrB is probably silent, the mlrA gene is a better molecular probe than mlrB for detecting or monitoring dynamics of microcystin-degrading bacteria. This research was supported by the State Key Basic Research and Development Plan of China (2008CB418002), the National Water Science and Technology Projects (2009ZX07101-013-02) and the Talent Scientist Program of the Chinese Academy of Sciences (082303-1-501). Fig. S1. Neighbor-joining trees constructed from the 16S rRNA gene (left) and the mlrA gene sequences (right) of microcystin-degrading MLN2238 ic50 bacteria. Bootstrap values are indicated at nodes. Please note: Wiley-Blackwell is not responsible for the content Alisertib order or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article. “
“The transition metal iron is an important element for the sustenance of life – it can function

either as an electron acceptor or as a donor and serves as a cofactor in many enzymes activities. The cytoplasmic NAD(P)H-dependent ferric reductase in Thermus scotoductus SA-01 shares high sequence and structural similarity to prokaryotic thioredoxin reductases. Here Wilson disease protein we report the sequence of the ferric reductase (which is typically annotated as a thioredoxin reductase-like protein) and a comparative

kinetic study with the thioredoxin reductase from SA-01. Structurally, the most noteworthy difference, immediately apparent from the protein sequence, is the absence of the disulphide redox centre in the ferric reductase. This is the first report relating the attributes of such a redox protein to its ability to reduce a ferric substrate. The transition metal, iron, is an important element for most organisms and is required for various physiological functions such as transport of molecular oxygen, involvement in electron transport and a cofactor for enzymes, and functions either as an electron donor or as an acceptor in microbial energy conservation. The dissimilatory reduction of ferric iron is considered the oldest form of respiration, thus providing an electron sink while the earth’s atmosphere was still anoxic (Vargas et al., 1998). Ironically, with the arrival of oxygen, iron posed a new threat to aerobically respiring organisms. Various redox-active biomolecules have been implicated in the cytotoxic effect of iron in aerobic respiring organisms by reducing the cellular ferric iron, which can then participate in the Fenton reaction. The successive univalent reduction of molecular oxygen, during aerobic respiration, generates superoxide (O2·−), hydrogen peroxide (H2O2) and hydroxyl (HO·) radicals, with the latter being most cytotoxic.

American Type Culture Collection (ATCC), food and clinical isolates, of

Gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa, Pseudomonas mirabilis), Gram-positive bacteria (Listeria monocytogenes, Enterococcus hirae, Enterococcus faecium, Bacillus subtilis, Staphylococcus epidermidis, Staphylococcus aureus), the yeasts Candida albicans and Candida parapsilosis and the fungus Aspergillus niger were used. Pistachio extracts were active against Gram-positive bacteria with a bactericidal effect observed against L. monocytogenes (ATCC strains and food isolates), S. aureus and MRSA clinical LDK378 nmr isolates. Extracts from raw shelled pistachios were more active than those from roasted salted pistachios. The bactericidal activity of pistachio extracts could be used to help control the growth of some microorganisms in foods to improve safety and may find application as a topical treatment for S. aureus. “
“Infections with non-typhoidal Salmonella strains are constant and are a non-negligible Tamoxifen threat to the human population. In the last two decades, salmonellosis outbreaks have increasingly been associated with infected fruits and vegetables. For a long time,

Salmonellae were assumed to survive on plants after a more or less accidental infection. However, this notion has recently been challenged. Studies on the infection mechanism in vegetal hosts, as well as on plant immune systems, revealed an active infection process Bay 11-7085 resembling in certain features the infection in animals. On one hand, Salmonella requires the type III secretion systems to effectively infect

plants and to suppress their resistance mechanisms. On the other hand, plants recognize these bacteria and react to the infection with an induced defense mechanism similar to the reaction to other plant pathogens. In this review, we present the newest reports on the interaction between Salmonellae and plants. We discuss the possible ways used by these bacteria to infect plants as well as the plant responses to the infection. The recent findings indicate that plants play a central role in the dissemination of Salmonella within the ecosystem. “
“Although DNA is the ultimate repository of biological information, deployment of its instructions is constrained by the metabolic and physiological status of the cell. To this end, bacteria have evolved intricate devices that connect exogenous signals (e.g. nutrients, physicochemical conditions) with endogenous conditions (metabolic fluxes, biochemical networks) that coordinately influence expression or performance of a large number of cellular functions. The phosphoenolpyruvate:carbohydrate-phosphotransferase system (PTS) is a bacterial multi-protein phosphorylation chain which computes extracellular (e.g. sugars) and intracellular (e.g. phosphoenolpyruvate, nitrogen) signals and translates them into post-translational regulation of target activities through protein-protein interactions.

American Type Culture Collection (ATCC), food and clinical isolates, of

Gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa, Pseudomonas mirabilis), Gram-positive bacteria (Listeria monocytogenes, Enterococcus hirae, Enterococcus faecium, Bacillus subtilis, Staphylococcus epidermidis, Staphylococcus aureus), the yeasts Candida albicans and Candida parapsilosis and the fungus Aspergillus niger were used. Pistachio extracts were active against Gram-positive bacteria with a bactericidal effect observed against L. monocytogenes (ATCC strains and food isolates), S. aureus and MRSA clinical see more isolates. Extracts from raw shelled pistachios were more active than those from roasted salted pistachios. The bactericidal activity of pistachio extracts could be used to help control the growth of some microorganisms in foods to improve safety and may find application as a topical treatment for S. aureus. “
“Infections with non-typhoidal Salmonella strains are constant and are a non-negligible Wnt inhibitor threat to the human population. In the last two decades, salmonellosis outbreaks have increasingly been associated with infected fruits and vegetables. For a long time,

Salmonellae were assumed to survive on plants after a more or less accidental infection. However, this notion has recently been challenged. Studies on the infection mechanism in vegetal hosts, as well as on plant immune systems, revealed an active infection process filipin resembling in certain features the infection in animals. On one hand, Salmonella requires the type III secretion systems to effectively infect

plants and to suppress their resistance mechanisms. On the other hand, plants recognize these bacteria and react to the infection with an induced defense mechanism similar to the reaction to other plant pathogens. In this review, we present the newest reports on the interaction between Salmonellae and plants. We discuss the possible ways used by these bacteria to infect plants as well as the plant responses to the infection. The recent findings indicate that plants play a central role in the dissemination of Salmonella within the ecosystem. “
“Although DNA is the ultimate repository of biological information, deployment of its instructions is constrained by the metabolic and physiological status of the cell. To this end, bacteria have evolved intricate devices that connect exogenous signals (e.g. nutrients, physicochemical conditions) with endogenous conditions (metabolic fluxes, biochemical networks) that coordinately influence expression or performance of a large number of cellular functions. The phosphoenolpyruvate:carbohydrate-phosphotransferase system (PTS) is a bacterial multi-protein phosphorylation chain which computes extracellular (e.g. sugars) and intracellular (e.g. phosphoenolpyruvate, nitrogen) signals and translates them into post-translational regulation of target activities through protein-protein interactions.