Surface chemical modifications significantly influence the performance of surface chemistry-derived devices such as optoelectronic devices, luminescent

devices, biosensors, and biomaterials. This work develops a novel method for detecting immunological diseases, in which terminal groups (-COOH) are modified and carboxyl groups on GOS surfaces are activated. The carboxyl groups of a GOS film can be converted into amine-reactive groups to increase its surface area sensing. Furthermore, modifying the oxygen-containing functional groups on the surface of GOS can increase its bandgap and its dielectric constant, thereby improving its surface plasmon resonance PI3K inhibitor (SPR) properties. Methods Figure 1a,b shows the design of two sensing chips, i.e., a BAY 11-7082 datasheet conventional SPR chip and a GOS film-based SPR chip. Standard SPR thin films were deposited with thin film for gold (Au) thickness of 47 nm and chromium (Cr) OTX015 mouse thickness of 2 nm on BK7 glass substrate to a thickness of 0.17 mm. SPR experiments were conducted using a BI-3000G SPR system with Kretschmann prism coupling (Biosensing Instrument, Tempe, AZ, USA). The test injection sample volume was 200 μl and the flow rate was 60 μl/s. All experiments were performed at 25°C and repeated in triplicate. Figure 1 SPR biosensor chip using an immunoassay method for detecting a protein using a gold binding. (a) Conventional

SPR chip and (b) GOS film-based SPR chip. Intensity of an evanescent field with a depth of approximately 100 ~ 500 nm decays

exponentially with increasing distance from the metal. Bimolecular binding, observed within approximately 10 nm of the metal surface, gives rise to a higher signal shift response than that of the interactive process at a distance of 300 nm therefrom. For typical SPR Kretschmann prism coupling that uses a red light to induce the evanescent field, its field intensity is no more than 600 nm in practice. Designed configuration for sensing Figure 1a presents Farnesyltransferase a conventional SPR sensing chip and a biomolecule binding mechanism. 8-Mercaptooctanoic acid (MOA; Sigma-Aldrich Co. LLC., St. Louis, MO, USA) is activation of carboxylic acid-terminated thiol self-assembled monolayers (SAMs) on a modified Au surface. MOA binds to the Au surface through their thiol linker (-SH end) resulting monolayers, which are terminated with carboxylic acid (-COOH). The MOA can be further functionalized to immobilize a bovine serum albumin (BSA; Sigma, Chemical Company, St. Louis, MO, USA) protein. Anti-BSA protein interactions are performed as well. Figure 1b shows a GOS film-based SPR chip with its biomolecule binding mechanism. Two binding mechanisms are functionalized SAMs on amino-modified Au surfaces by solutions of cystamine (Cys; Alfa Aesar Co., Ward Hill, MA, USA) with a concentration of 5 mM and octadecanthiols (ODT, C18H37SH; Sigma-Aldrich Co. LLC.) with a concentration of 10 mM formation of Au-S bonds that immobilize a GOS.

Endpoints The primary endpoint was the change in clinic systolic and diastolic BP after 6 months of treatment. Secondary endpoints included change in home BP, urinary albumin creatinine excretion ratio (ACR), B-type natriuretic peptide (BNP) and serum UA concentration. BP measurements and laboratory tests The clinic BP was measured in a sitting position during a morning visit (9–11 am) every 4 weeks. We followed all American

Heart Association Recommendations published in 1988 [8, 10] including using a 47 × 13 cm cuff and 24 × 13 cm bladder to avoid cuff hypertension. The cuff was strictly positioned 2 cm above the antecubital crease to obtain a similarly leveled complete compression of the brachial artery. All BP values were expressed as the average of two measurements obtained at the same time-point. Patients were VX-680 required to measure home BP in the morning in a sitting SB431542 order position within 30 min after awakening before taking medications in a fasting state. Night time home BP measurement was also required to measure at any given

time between supper and bedtime with having patient’s habitual drinking unrestricted. BP measuring devices equipped with upper arm cuff were encouraged to use. The averages of several measured values GSK2126458 ic50 were used for analysis. Laboratory tests carried out after 6 months of treatment were BNP, serum Cr concentration, ACR, estimated-GFR (eGFR), serum UA concentration, and others including lipid profiles. The urinary albumin level was

determined from a spot urine sample using a turbidimetric immunoassay (SRL, Tokyo, Japan). Plasma BNP was measured using high-sensitivity, noncompetitive radioimmunoassays (Shiono-RIA BNP, Shionogi Inc, Osaka, Japan) Statistical analyses The paired student’s t test, Wilcoxon’s signed rank test, and one-way analysis of variance (ANOVA) and Bonferroni’s post hoc test were carried out with JMP 9.0 software. The computer used for the analysis was a Dynabook Satellite 2590X (Toshiba, Tokyo, Japan). Data are presented as the mean ± standard deviation Florfenicol (SD) for continuous variables with normal distribution. Continuous variables without normal distribution are presented as median and interquartile range (IQR) with 25 and 75 percentiles. Because of their skewed distribution, logarithmic transformation of BNP and ACR values were performed as the geometric means with 95% confidence intervals. A P value of less than 0.05 was considered statistically significant. Results Prescription of antihypertensive agents A total of 277 patients were registered in the JOINT study, of whom 49 were excluded (33 were lost during follow-up, 7 had protocol violations, and 9 had inadequate data for analyses). Consequently a total of 228 patients with clinical index data were included in the analysis.

The slight difference may be caused by the tiny difference in the battery package pressure by manual operation or the tiny difference in the amount of electrolyte added to the Li/MnO2 cells by manual operation. Considering the tiny difference in manual operation, the small difference of R s is acceptable

since the ohmic electrolyte resistances of the MnO2 micromaterials are similar. The R sf and R ct of the urchin-like MnO2 are much lower than that of the caddice-clew-like MnO2. It proves that the Li-ion migration resistance through the SEI films and charge transfer resistance of the urchin-like MnO2 are much lower than that of the caddice-clew-like MnO2. Here, the influence of the tiny difference in the battery package pressure and the amount of electrolyte on the R sf and R ct can be neglected. So, the urchin-like Selleckchem Cobimetinib morphology is more favorable for lithium ion click here diffusion and transfer, and the reaction of MnO2 micromaterials with lithium ion is much easier. Table 1 R s , R sf , and R ct calculated from Nyquist plots for the MnO 2 materials   R s (Ω cm2) R sf (Ω cm2) R ct (Ω cm2)

a 8.05 121.40 146.90 b 7.12 94.66 43.64 a, caddice-clew-like MnO2 sample; b, urchin-like MnO2 sample. Conclusions In summary, two MnO2 micromaterials with urchin-like and caddice-clew-like Pritelivir chemical structure morphologies are prepared by hydrothermal method. Both the crystalline phases are α-MnO2, which is essential to evaluate the relationship between electrochemical performances and morphologies of MnO2 crystals as anodes for lithium-ion battery application. Both the as-prepared α-MnO2 exhibit high initial specific capacity, but the discharge cycling stability is poor. Just in case of this research, the urchin-like MnO2 material has better electrochemical performance. The results suggest that different morphologies indeed have influence on electrochemical performances of MnO2 micromaterials in the application of lithium-ion battery. This study also gives us advice to make shell coating on the as-prepared

MnO2 micromaterials to improve the cycling stability. Acknowledgements This work was financially supported by the Program for Innovative Research Team (in Science and Technology) in the University of Yunnan Province (2010UY08, 2011UY09), Yunnan Megestrol Acetate Provincial Innovation Team (2011HC008), the General Program of the Application and Basic Research Foundation of Yunnan Province (2013FZ080), the Youth Fund Research Project of Yunnan Minzu University (2012QN01), the Key Project of Scientific Research Foundation of the Educational Bureau of Yunnan Province (2013Z039), and the Graduate Program of Scientific Research Foundation of the Educational Bureau of Yunnan Province (2013J120C). References 1. Sui N, Duan Y, Jiao X, Chen D: Large-scale preparation and catalytic properties of one-dimensional MnO 2 nanostructures. J Phys Chem C 2009, 113:8560–8565.CrossRef 2.

The complementary morphology of hollow silicon nanotubes (SiNTs) also provides opportunities in areas such as battery technology, photovoltaics, as well as drug delivery. SiNTs are tunable in their inner diameter as well as in their wall-thicknesses [3]. They provide a uniform structure compared to the dendritic pore growth of porous silicon in the target porous regime (30 to

90 nm pore diameter), and therefore, such structures are attractive for infiltration with nanoparticles or molecules (e.g., superparamagnetic (SPM) iron Enzalutamide supplier oxide nanoparticles of the form Fe3O4). In terms of possible candidates for this website loading, superparamagnetic Fe3O4 nanoparticles (NPs) also offer a low toxicity and thus can be applied to diverse uses in biomedicine, e.g., for hyperthermia, NMR imaging, and functionalization with anti-cancer agents [4]. In this work, SiNTs are infiltrated with Fe3O4 NPs to achieve a nanocomposite system which can, in the long term, be considered for use as a magnetic-assisted drug delivery vehicle. Previously, porous silicon loaded with iron oxide NPs of different sizes has been investigated with the cytocompatibility of this system showing encouraging results [5]. The cytocompatibility of SiNTs

has also been recently evaluated [6]. In the following work, the infiltration of Fe3O4 NPs into SiNTs of different wall thicknesses is described and the fundamental magnetic properties of these composites investigated as a function of the Fe3O4-nanoparticle size. Methods Silicon nanotubes were fabricated by a multistep process PF-04929113 supplier previously described [3] involving deposition of silane (SiH4) on preformed ZnO nanowire array templates on F-doped tin oxide (FTO) glass or Si wafer segments, followed by sacrificial etching of the ZnO phase resulting

in the desired nanotube product. Hollow nanotube inner diameter is adjustable by size selection of the initial ZnO nanowire template, while shell thickness control is achieved by concentration/duration second of silicon deposition. In these experiments, SiNTs with 10-nm wall thickness are obtained at 530°C with a 5-min Si deposition time, and SiNTs with 70-nm wall thickness are obtained at 580°C with a 5-min Si deposition time. Internal nanotube diameter is dependent on ZnO nanowire diameter, which in the experiments described here, is fixed at 50 nm. The wall thickness determines the dissolution of the material in vitro and thus is of importance for controlled drug release (vide infra). Iron oxide NPs have been prepared by a known route utilizing decomposition of an iron complex at high temperature [7]. NPs of different sizes (4 and 10 nm) are infiltrated into SiNTs with 10- and 70-nm wall thicknesses. The infiltration process performed at room temperature is supported by a magnetic field to assure optimal filling of the nanotubes. The infiltration process has been optimized with respect to the wall-thickness of the SiNTs and the size of the NPs used.

1967; Ward and Lawler 1967). Soon, CIDNP has been also observed in a photochemical reaction (Cocivera 1968). The term “photochemical induced dynamic nuclear polarization (photo-CIDNP)” refers to this specific photochemical

origin of the phenomenon. CIDNP has been explained by the radical pair mechanism (RPM) (Closs and Closs 1969; Kaptein and Oosterhoff 1969). This mechanism is caused by different nuclear spin sorting leading to different chemical fates of the products. Due to coherent S-T0 mixing, upon inter-system crossing (ISC) the spin state of the radical pair is oscillating between a singlet- and a triplet-state. The radicals forming a singlet-radical pair may recombine, while the triplet products are forced to diffuse apart. Hence, this mechanism requires mobility and can build-up

VX 770 CIDNP only in the fluid phase. Later, the mechanism has been extended to S-T+ and S-T− mixing as well, for example occurring in biradicals and at low fields (Closs and Doubleday 1972; de Kanter et al. 1977). In addition, also an electron–nuclear Overhauser cross-relaxation mechanism click here operating in liquid state has been observed, (Adrian 1974; Closs 1975) which also RG-7388 explains polarization buildup in cyclic reactions (Closs et al. 1985). In a triplet Overhauser mechanism (Adrian 1977) nuclear polarization is created upon ISC from an excited singlet- to a triplet-state. While the RPM is based on fast coherent evolution of an electron–electron–nuclear spin system and spin state sorting in alternative reaction pathways, the Overhauser mechanism relies on usually slower incoherent cross relaxation that transfers polarization from electrons to nuclei. The latter mechanism requires a matching of the cross-relaxation time to the life time of the radical

pair, while transient polarization from the RPM cancels under steady-state conditions for cyclic reactions. In the same Cobimetinib solubility dmso time, two other spin-chemical phenomena were discovered in photosynthetic systems: (i) photochemically induced dynamic electron polarization (photo-CIDEP), which is enhancement of EPR signals upon illumination, has been observed in chloroplasts (Blankenship et al. 1975) and RCs of purple bacteria (Hoff et al. 1977a) (ii) the magnetic field effect (MFE) on the triplet yield was discovered in bacterial RCs (Blankenship et al. 1977; Hoff et al. 1977b). Although the exact mechanism was not understood, both phenomena were interpreted in terms of magnetic-field dependent interactions of electrons with nuclei (Hoff et al. 1977b; Werner et al. 1978; for review: Hoff 1984). Based on this assessment, “new classes of experiments” were predicted for NMR (Goldstein and Boxer 1987). In 1994, Zysmilich and McDermott observed for the first time this new type of photo-CIDNP in frozen and quinone-blocked RCs of purple bacteria of Rb. sphaeroides R26 (Zysmilich and McDermott 1994).

A. Alignment of the DNA sequences of the intergenic region between the cacA-coding region and its upstream ORF (STM1851) in E. coli (ECO), C. koseri (CKO), Enterobacter sp. 638 (ENT), S. enterica serovar Typhimurium LT2 (STM), Klebsiella pneumoniae

(KPN), and C. sakazakii (ESA). Asterisks correspond to nucleotides that are conserved in all listed species. Twin dots and single dots indicate conservative and semiconservative substitutions, respectively. The -10 region sequence is marked in bold blue letters. The bent arrow indicates the transcription start site (TSS) of the cacA transcript, as determined by a recent report [30] (designated position +1). The inverted arrows indicate predicted Rho-independent terminator sequences. The initiation codons for the cacA gene are boxed. find more INCB018424 mouse B. Designated

mutations in the cacA promoter. The -10 region sequence (CTA cac T from -13 to -7) [29] represents a consensus sequence that is recognized by RpoS. The -10 region sequence of the cacA promoter is highlighted in blue. The numbers shown above the wild-type sequence are the positions relative to the cacA TSS [30]. The Selleckchem PD 332991 substituted nucleotides (-14C/G, -16T/A -14C/G, and -12A/T -8T/A) are underlined. C. β-galactosidase activity from a P cacA -lac transcriptional fusion 2 in the wild-type (−; AK1067), ΔrpoS mutant (AK1071), -14C/G cacA promoter mutant (AK1068), ΔrpoS -14C/G cacA promoter mutant (AK1072), -16T/A -14C/G cacA promoter mutant (AK1069), ΔrpoS -16T/A-14C/G cacA promoter mutant (AK1073), -12A/T -8T/A cacA promoter mutant (AK1070), and ΔrpoS -12A/T -8T/A cacA promoter mutant (AK1074) strains. Bacteria were grown for 4 h in LB before β-galactosidase activity was measured (arbitrary units) as described [42]. The data correspond to the means of three

independent experiments performed in duplicate, and the error bars represent standard deviations. HA-1077 Moreover, although the location of the predicted -10 region correlates well with a transcription start site (TSS) determined by a genome-scale precise mapping of TSSs that covered 78% of the Salmonella ORFs [30], no obvious typical -35 region sequence exists upstream of the -10 nucleotides (Figure 3A). We mutated this -10 sequence from TCCTACACT to TCG TACACT (-14C/G), ACG TACACT (-16T/A-14C/G), or TCCT T CAC A (-12A/T -8T/A) and analyzed their effects on cacA transcription (Figures 3B and 3C). In the ΔrpoS mutant, the β-galactosidase activity of the cacA promoter was approximately 1/3 of wild-type levels (Figure 3C). However, the β-galactosidase activities from the cacA promoter containing -14C/G or -16T/A -14C/G substitutions were not affected by the ΔrpoS mutation after 4 h of growth in LB, indicating that these substitution mutations rendered the cacA promoter RpoS-independent (Figure 3C).

Their study, carried out in a healthcare setting, demonstrated that organizational support moderated Sirolimus the effects of physical violence, vicariously experienced violence, psychological assault on emotional well-being, somatic health and job-related affect. Cole et al. (1997) showed that reduced supervisory

support was associated with harassment, threats and fear of violence in the workplace. Our study points to the fact that employer support of employees is likely to be crucial to their recovery from a workplace violence event in a large variety of professions. Past research has often concentrated on one type of occupation, for instance in the healthcare sector (Gates 2004). Our study has implications for the prevention of consequences of workplace violence by such interested parties as employers, occupational health and healthcare providers as well as victims’ services organizations. Based on our findings, the psychological distress of victims shortly after a violent event, even in the absence of serious physical

injuries, should not be underestimated and victims should be advised selleck screening library to seek professional help. Moreover, the importance of support from employers for the recovery of workplace violence victims needs to be emphasized. In the qualitative section of our study (De Puy et al. 2012), respondents gave examples of forms of support from employers that had been particularly helpful.

This included moral support and follow-up (a phone call, a letter, or a visit to the hospital), assisting the victim in order to obtain medical care, legal and administrative Clomifene advice (filing a complaint, or getting insurance benefits), and organizational measures to prevent future incidents (hiring security guards, improving protective procedures, banning the perpetrator from the premises or check details signaling the perpetrator to the staff). In contrast, interviewees who had not received any of these forms of support or had experienced the employer’s response as inadequate (e.g., victim blaming, being dismissed) expressed strong feelings of disappointment and distress. We found that first-time victimization appears as a risk factor for more severe consequences in occupations with high risk and awareness of violence. This unexpected result would need to be verified in further studies with larger samples. However, it is possible that successful recovery and subsequent return to work after the violent encounter is the key factor rather than the number of times a violent incident is experienced. The limitations of our study are inherent to the clinical nature of our population. The size of our sample was determined by the number of people who came to the consultation between 2007 and 2010 following a workplace violence event.

AgNPs have been currently applied as disinfecting agents in general practice due to their antibacterial effects (http://​www.​nanotechproject.​org/​inventories/​consumer/​analysis_​draft/​). Therefore, antibacterial activity of the resulted AgNP solutions, namely

AgNPs/PVA, AgNPs/PVP, AgNPs/sericin, and JPH203 AgNPs/alginate was tested. Figure 3 displayed the dynamics of bacterial growth in liquid LB medium supplemented with 107 E. coli cells/100 mL and 1-mg/L AgNPs in different stabilizers. OD o and OD t (Figure 3) are the optical density values of the studied sample solutions at the beginning and at the different contacting time, respectively. In all AgNP-treated samples, the AgNPs caused a growth delay of E. coli compared with the control sample, and the growth delay effect was different in the following sequence: AgNPs/alginate (7.6 nm) > AgNPs/PVA (6.1 nm) > AgNPs/PVP (4.3 nm) > AgNPs/sericin (10.2 nm). The obtained results also proved that the antibacterial effect of AgNPs depends not only on the size but also on the stabilizer used. Figure 3 The growth curves of E. coli exposed to the colloidal AgNPs in different stabilizers. In addition, Sondi and Salopek-Sondi [25] and Tiwari et al. [22] reported that the

concentration of AgNPs is mainly responsible for the antibacterial effect along with treatment time. Moreover, Selleck ABT-888 the results of El Badawy et al. have also confirmed that the stabilizers of the AgNPs were one of the most important Phospholipase D1 determinants of the antibacterial activity of AgNPs [20]. For that reason, upon each application purpose, the appropriate stabilizer should be chosen for capping AgNPs, especially for applying AgNPs as antibacterial agents. Therefore, in

this study, an antibacterial handwash solution was prepared using Na-LS as surfactant, HEC as binder, and 15 mg/L of AgNPs/alginate as antimicrobial agent. selleck screening library Photographs of handwash solutions and bactericidal activity were showed in Figure 4. The handwash without AgNPs (HW) was almost non-antibacterial against E. coli; the η value reached approximately 6.2% only. The bactericidal efficiency with only 3-mg/L AgNPs diluted from the handwash solution against E. coli with a bioburden of approximately 107 CFU/100 ml (E. coli infection is much higher in comparison with real conditions) was 74.6%, 89.8%, and 99.0% for 1, 3, and 5 min of contacting time, respectively (Table 2). Figure 4 Photograph of handwash containing AgNPs and the growth of E. coli in LB agar with time. Table 2 The bactericidal efficiency ( η ) of handwash/AgNPs with contacting time Time E. coli (CFU/mL) η (%) Control (LB) 33.9 × 105 – Control (HW) 31.8 × 105 6.2 1 min 86.0 × 104 74.6 3 min 34.6 × 104 89.8 5 min 3.3 × 104 99.0 Wei et al. also reported the high bactericidal effect of AgNPs with sizes of 6 to 8 nm against E. coli, particularly the η value of 10-mg/L AgNPs which was approximately 99.9% for 2 min of contacting time [11].

Since the end point of CFU assay is the formation of fungal colonies by individual cells, growth inhibition without killing would go undetected. Nonetheless, the fact that we washed the treated cells extensively with sterile distilled water makes it unlikely that in PRT062607 supplier our experiments the fungal cells were only inhibited by the bacterial cells without killing them. Our results show that the monomicrobial and the polymicrobial biofilms of A. fumigatus and A. fumigatus-P.

aeruginosa were almost equally susceptible to antifungal drugs such as voriconazole and posaconazole. The main reasons for the biofilm to exhibit drug resistance/tolerance are (1) biofilm specific upregulation of efflux proteins (2) the presence of an extracellular matrix and (3) the presence of persistor cells that are inherently drug resistant/tolerant due to their low https://www.selleckchem.com/products/Dasatinib.html metabolic rate. It is likely that there is no differential upregulation of efflux proteins in monomicrobial and polymicrobial biofilms of A. fumigatus and A. fumigatus-P. aeruginosa. Similarly, although it is possible that the extracellular matrix produced by monomicrobial and VE-821 purchase polymicrobial biofilms of A. fumigatus and A. fumigatus-P. aeruginosa mixed culture is different, the difference in the permeability characteristics of monomicrobial and polymicrobial biofilm produced extracellular matrices are not sufficient enough to show any reduction in drug penetration.

Since the growth characteristics and the biology of A. fumigatus is vastly different from other unicellular organisms such as bacteria and pathogenic yeasts, the presence of persistor cells 3-mercaptopyruvate sulfurtransferase inherently resistant to antimicrobial drug is highly unlikely. Together, these points suggest that although differential antifungal drug susceptibility for A. fumigatus monomicrobial and polymicrobial biofilms was expected, the lack of such response is not entirely surprising. In contrast, our antimicrobial drug susceptibility studies

showed that polymicrobial biofilm associated P. aeruginosa cells are less susceptible to cefepime in comparison to their monomicrobial counterparts. The extracellular matrix of P. aeruginosa biofilm is composed of proteins, polysaccharides, in particular alginate, and eDNA whereas that of A. fumigatus biofilm is made up of galactomannan, alpha-1,3 glucans, monosaccharides and polyols, pigments, proteins and eDNA. The most plausible explanation for the reduced susceptibility of polymicrobial biofilm embedded P. aeruginosa is the difference in the make up of the extracellular matrix of monomicrobial (P. aeruginosa) and mixed microbial (P. aeruginosa-A. fumigatus) biofilms. The polymicrobial extracellular matrix may have permeability properties different from that of the monomicrobial extracellular matrix preventing adequate access to the biofilm embedded cells. Conclusions The high prevalence of P. aeruginosa and A.

90%, 10.57%, selleck inhibitor and 17.68%, in LB with 0, 150, and 300 mM NaCl, respectively). While the mutant had less invasion efficiency, the result clearly demonstrated that increasing salt concentration from 0 to 150 or 300 mM NaCl led to significantly improved invasion of B. pseudomallei mutant into A549 cells as it is observed for the wild type strain (Figure 2). Figure 2 Invasion of A549 epithelial

cells by B. pseudomallei. A549 cells were infected with overnight cultures of B. pseudomallei K96243 at MOI of 100, SDO mutant, and Idasanutlin mw complement strains grown in NaCl-free LB broth, LB broth with 150 mM NaCl, or LB broth with 300 mM. Intracellular bacteria were counted after lysing infected cells at 4 hrs post-infection. Asterisks indicate significant differences (p-value ≤ 0.05, t-test) between groups. Error bars represent standard errors of mean for experiments performed in triplicate. The ability of B. pseudomallei to survive and replicate intracellularly AZD2014 in vitro may be attributable

to the successful evasion of cellular killing strategies. We next examined the intracellular survival of the B. pseudomallei wild type and the SDO mutant within macrophages. The macrophage cells were chosen for this experiment because B. pseudomallei can be uptaken and multiply within these cells, and resist their bactericidal response [21, 22]. The mutant showed fewer intracellular bacteria within the J774A.1 macrophage cell line during the initial stages of infection – up to 6 hrs (p -value ≤ 0.05) (Figure 3). The intracellular doubling time of the B. pseudomallei SDO mutant pre-exposure to 0, 150, and 300 mM NaCl was 41.83 ± 1.71, 45.41 ± 2.66, and 50.41 ±

1.33%. In contrast, the doubling time of the wild type bacteria fantofarone was 32.50 ± 4.29, 36.39 ± 1.44, and 47.23 ± 2.31% in LB with 0, 150, and 300 mM NaCl. The SDO complement strain recovered the growth of the SDO mutant with a rate similar to the wild type at an early time. Our data suggests that SDO plays an important role during the early phase of B. pseudomallei infection. It is possible the mutagenesis of SDO impaired the invasion of B. pseudomallei into A549 epithelial cells, and delayed initial multiplication within J774A.1 macrophage cells. Figure 3 Intracellular survival of B. pseudomallei in J774A.1 macrophages. J774A.1 cells were infected with overnight cultures of B. pseudomallei K96243 at MOI of 2, SDO mutant and complement strain grown in NaCl-free LB broth, LB broth with 150 mM NaCl, or LB broth with 300 mM. Intracellular bacteria were counted after lysing infected cells at 3, 6 and 9 hrs post-infection. Asterisks indicate significant differences (p-value ≤ 0.05, t-test) between groups. Error bars represent standard errors of mean for experiments performed in triplicate. SDO is not essential for B.