Table 1 Sampling

site locations and characteristics Code Site name (GISb map reference) check details Site characteristics C1 Coomera marina (-27.861672, 153.339089) Cattle/kangaroo feeding, house-boat mooring site C2 Santa Barbara (-27.855165, 153.350612) Well used park, BBQ, toilets and fishing, private houses about 100 m away C3 Sanctuary Cove (-27.851617, 153.362140) Canal estate, modern houses and apartments, modern infrastructure, commercial/light industrial area C4 Jabiru Island (-27.879057, 153.380685) Busy through road, disused sand mine, no houses, small park with toilets C5 Paradise Point (-27.886359, 153.396596) Public swimming area, mouth of river, LBH589 cell line much water traffic C6 Coombabah, Estuary (-27.896607, 153.366845) Established suburban area, bush island opposite b Global information system Water samples were collected in sterile bottles according to the sampling procedures described in the USEPA microbiology methods manual [9]. The sampling depth for surface water samples were 6-12 inches below the water surface. Samples were transported in a cooler on ice packs to the laboratory where they were prepared for analyses immediately upon arrival and were tested within 6 h of collection for the presence of enterococci. Isolation

and identification of enterococci The environmental water samples were mixed thoroughly, and undiluted samples or a 1:10 dilution of water samples were filtered through 0.45 μm membrane filters (MilliporeCorporation, Interleukin-2 receptor Bedford, MA, USA), placed onto membrane-Enterococcus Indoxyl β-D-Glucoside Agar (mEI) (Becton-Dickinson, Sparks, MD, USA) according to the USEPA specifications [30]. Triplicate samples were collected from each site and each sample was treated separately. The addition of Indoxyl-β-D-Glucoside, Nalidixic acid, 0.1 N NaOH, and Triphenyltetrazolium Chloride to mEI agar

(Difco) allowed for a single 24 h incubation period at 41°C [31]. E. faecium ATCC 27270, E. faecalis ATCC 19433 and E. coli ATCC 25922 were used as positive and negative controls respectively to validate the mEI agar. Colonies producing a blue halo were typically observed for enterococci and counted, the result expressed as cfu/ml for each water sample. Statistical analysis The Mann-Whitney U-test at 5% significance level was performed to determine whether there was a significant increase of total enterococcal counts (cfu/ml) at each location after rainfall events. Identification of E. faecium and E. faecalis Typical colonies on the membranes were identified to the genus and species level by Gram-stain, catalase test, the ability to tolerate 6.5% NaCl and biochemical tests [32]. The isolates identified as E. faecium and E.

Furthermore, fifty-five out of the 147 ArcA-activated genes (37%), and 100 out of the 245 ArcA-repressed genes (41%) contained at least one putative ArcA-binding site (Additional file 1: Table

S1). Figure 2 Logo of the information matrix obtained from the alignment of ArcA sequences for S . Typhimurium. Sequences were obtained by searching the S. Typhimurium LT2 genome [Accession #: AE006468 (chromosome) and AE606471 (plasmid)] with known ArcA sequences derived from the corresponding ArcA-regulated genes in E. coli. A total of 20 E. coli sequences were used to obtain the logo shown. The total height of each column of characters represents the amount of information [measured in bits, which is the maximum entropy for buy PXD101 the given sequence www.selleckchem.com/products/SB-203580.html type (ex. Log2 4 = 2 bits for DNA/RNA and log2 20 = 4.3 bits for proteins)] for that specific position and the height of each individual character represents the frequency of each nucleotide. ArcA as a repressor Transcription of the genes required for aerobic metabolism, energy generation, amino acid transport,

and fatty acid transport were anaerobically repressed by ArcA (Additional file 1: Table S1). In particular, the genes required for cytochrome-o-oxidase, succinyl-CoA synthetase, glutamate/aspartate transport, trehalose-6-phosphate biosynthesis, long-chain fatty acids transport, spermidine/putrescine transport, dipeptide transport, the genes encoding the two-component tricarboxylic transport system and the site-specific DNA factor for inversion stimulation (fis) were among the

highest repressed by ArcA. Genes required for L-lactate transport and metabolism, phosphate transport, acetyl-CoA transferase, APC family/D-alanine/D-serine/glycine transport, putative cationic amino acid transporter, peptide methionine sulfoxide reductase, multiple antibiotic resistance Morin Hydrate operon, as well as many poorly characterized genes were also repressed by ArcA (Additional file 1: Table S1). Additionally, some genes related to Salmonella virulence were repressed by ArcA. For example, the expression of the mgtCB operon (member of SPI-3) that is required for Mg2+ transport/growth in low-magnesium and involved in systemic infections in mice/intramacrophage survival [37–40], genes constituting the lambdoid prophage Gifsy-1 that contributes to the virulence of S. Typhimurium [41], and genes coding for a leucine-rich repeat protein (sspH2) that is translocated by and coordinately regulated with the SPI-2 TTSS [42] were highly repressed by ArcA (Figure 3A and Additional file 1: Table S1). Figure 3 Organization of major genes for (A) SPI-3, (B) ethanolamine utilization, (C) propanediol utilization, and (D-F) flagellar biosynthesis and motility.

epidermidis (MTCC435) and P. aeruginosa (ATCC27853) in a microtiter plate assay in triplicates. To examine the bacterial growth or killing rate in the presence of different fractions, bacterial cells were grown in 100 μl of Mueller-Hinton

Proteasome inhibitor broth (MHB, HiMedia, India) supplemented with fixed concentration (10 μg/ml) of each fraction, at 37°C. Growth or killing rates were determined by measuring OD at 600 nm. The OD values were converted into concentration of cells measured in CFU per millilitre (1.0 OD corresponded to 2.16 × 108 CFU/ml). The MIC of selected biosurfactant/lipopeptide was evaluated for strains S. aureus (MTCC1430), M. luteus (MTCC106) and S. marcescens (MTCC 97) along with P. aeruginosa and S. epidermidis by using a microtiter plate dilution assay in triplicates as described earlier [48]. Test strains were grown to logarithmic phase (between 0.3-0.4 OD) under optimal conditions. The lowest concentration inhibiting the growth of test strain without showing any increase in absorption up to 48 h of incubation was considered as MIC. MALDI-TOF-MS and sequencing The purified and active lipopeptides were analysed for molecular mass and MS/MS sequencing by using a Voyager time-of-flight mass spectrometer (Applied Biosystems, Foster City, CA, USA). For MS/MS sequencing, the

Epigenetics inhibitor lactone ring present in lipopeptide was cleaved by incubating each peptide with 10% NaOH in methanol at room temperature for 16 h. The cleaved peptide obtained was lyophilized and again extracted with methanol, and allowed for

mass spectrometry analysis. Spectra were recorded in the post-source decay (PSD) ion mode as an average of 100 laser shots with a grid voltage of 75%. The reflector voltage was reduced in 25% steps and guide wire was reduced 0.02–0.01% with an extraction delay time of 100 ns. Fatty acid analysis by GC-MS To analyze the fatty acid content associated with the lipopeptides, the peptides (5 mg of each) were incubated with 0.5 ml of 6 M HCl at 90°C for 18 h in sealed tubes for acid hydrolysis. The fatty acids were extracted with ether, treated with 0.95 ml methanol and 0.05 ml of 98% H2SO4 at 65°C for 6 h. Finally, fatty acid methyl esters were obtained with n-hexane extraction these and analyzed on GC-MS with a Clarus 500 GC (PerkinElmer, USA). The carrier gas used was helium with a flow rate of 1.0 ml/min. The column temperature was maintained at 120°C for 3 min and thereafter gradually increased (8°C/min) to 260°C. Statistical analysis The statistical significance of the experimental results was determined using one-way ANOVA followed by Dunnett’s test. Values of p<0.05 were considered statistically significant. Prism version 5.0 was used for all statistical analyses. The results are presented as the mean of triplicates (n=3) ± SD.

FEMS Microbiol Lett 2008, 281:215–220.PubMedCrossRef 8. Bandi C, Anderson TJC, Genchi C, Blaxter ML: Phylogeny of Wolbachia in filarial nematodes. Proc Roy Soc Lond B 1998, 265:2407–2413.CrossRef 9. Bordenstein S, Rosengaus RB: Discovery of a novel Wolbachia supergroup in isoptera. Curr Microbiol 2005, 51:393–398.PubMedCrossRef 10. Casiraghi M, Bordenstein SR, Baldo L, Lo N, Beninati T, Wernegreen JJ, Werren JH, Bandi C: Phylogeny of Wolbachia pipientis based on gltA , groEL and ftsZ gene sequences: clustering of arthropod and nematode

symbionts in the F supergroup, and evidence for further diversity in the Wolbachia tree. Microbiol Osimertinib purchase 2005, 151:4015–4022.CrossRef 11. Lo N, Casiraghi M, Salati E, Bazzocchi C, Bandi C: How many Wolbachia supergroups exist? Mol Biol Evol 2002, 19:341–346.PubMedCrossRef 12. Ros VID, Fleming VM, Feil EJ, Breeuwer JAJ: How diverse is the genus Wolbachia ? Multiple-gene sequencing reveals a putatively new Wolbachia supergroup recovered from spider mites (Acari: Tetranychidae). Appl Environ Microbiol 2009, 75:1036–1043.PubMedCrossRef

13. Werren JH, Windsor D, Guo LR: Distribution of Wolbachia among neotropical arthropods. Proc Roy Soc Lond B 1995, 262:197–204.CrossRef 14. Chang J, Masters A, Avery A, Werren JH: A divergent Cardinium found in daddy long-legs (Arachnida: Opiliones). J invertebr Pathol 2010, 105:220–227.PubMedCrossRef Selleckchem Small molecule library 15. Duron O, Hurst GDD, Hornett EA, Josling JA, Engelstädter J: High incidence of the maternally inherited bacterium Cardinium in spiders. Mol Ecol 2008, Clostridium perfringens alpha toxin 17:1427–1437.PubMedCrossRef 16. Martin OY, Goodacre

SL: Widespread infection by the bacterial endosymbiont Cardinium in arachnids. J Arachnol 2009, 37:106–108.CrossRef 17. Perlman SJ, Magnus SA, Copley CR: Pervasive associations between Cybaeus spiders and the bacterial symbiont Cardinium . J Invert Pathol 2010, 103:150–155.CrossRef 18. Zchori-Fein E, Perlman SJ: Distribution of the bacterial symbiont Cardinium in arthropods. Mol Ecol 2004, 13:2009–2016.PubMedCrossRef 19. Enigl M, Schausberger P: Incidence of the endosymbionts Wolbachia , Cardinium and Spiroplasma in phytoseiid mites and associated prey. Exp Appl Acarol 2007, 42:75–85.PubMedCrossRef 20. Gotoh T, Noda H, Ito S: Cardinium symbionts cause cytoplasmic incompatibility in spider mites. Heredity 2006, 98:13–20.PubMedCrossRef 21. Nakamura Y, Kawai S, Yukuhiro F, Ito S, Gotoh T, Kisimoto R, Yanase T, Matsumoto Y, Kageyama D, Noda H: Prevalence of Cardinium bacteria in planthoppers and spider mites and taxonomic revision of “” Candidatus Cardinium hertigii”" based on detection of a new Cardinium group from biting midges. App Environ Microbiol 2009, 75:6757–6763.CrossRef 22. Baldo L, Ayoub NA, Hayashi CY, Russell JA, Stahlhut JK, Werren JH: Insight into the routes of Wolbachia invasion: high levels of horizontal transfer in the spider genus Agelenopsis revealed by Wolbachia strain and mitochondrial DNA diversity. Mol Ecol 2008, 17:557–569.PubMedCrossRef 23.

This large difference

indicates that the JAK/stat pathway unbinding events we have observed and analysed with photo-oxidised RCs involve the formation of the electron transfer complex between the cyt c 2 and RC-LH1-PufX proteins at some stage during our measurements. The results from our SMFS control experiments with a large excess of free cyt c 2-His6 in solution are consistent with this conclusion; here, the binding probability decreased by the same factor down to the level of the probability for a non-specific interaction. In the latter case, the residual binding probability in these control measurements can be attributed to the dynamic nature of the interaction between the RC-His12-LH1-PufX complex on the sample surface and the free cyt c 2-His6 in solution, which, Inhibitor Library chemical structure although in excess, still leaves the RC binding site unblocked for short periods and free to interact with surface-bound cyt c 2-His6 molecules. In the two types of AFM experiments performed here, PF-QNM and SMFS measurements, experimental parameters such as the tip–sample contact time (defined as the time interval between bringing

both molecules together and their complete separation), the approach and retract velocities of the AFM probe and the repetition rate of the measurement differ substantially, thus not always allowing for direct comparison between the data. During the PF-QNM measurement, the tip–sample contact time is approximately 160 μs and the repetition rate of the force measurements is 1 kHz. The tip–sample contact time is shorter than the half-life time of the bound state of the electron transfer complex, which is approximately 200–400 μs (Dutton and Prince 1978; Overfield et al. 1979). Moreover, the repetition rate of the force measurements is 1 kHz, higher than the maximum possible turnover rate,

which is in the range 270–800 s−1 (Gerencsér et al. 1999; Paddock et al. 1988). Thus, we can conclude that the PF-QNM measurements do not undersample the dissociation events but rather oversample them, indicating that PF-QNM experiments can access the transient Alanine-glyoxylate transaminase bound state of the electron transfer complex and measure the dissociation of its components. Nevertheless, we cannot distinguish between cyt c 2[ox]–RC[red] and cyt c 2[red]–RC[ox] interacting pairs, given that the duration of tip–sample contact of approximately 160 μs is much longer than the time taken for electron transfer (Overfield et al. 1979; Moser and Dutton 1988). The data presented in this article do, however, show that PF-QNM has the potential to investigate novel aspects of the formation, nature and dissociation of cyt c 2–RC-LH1-PufX interactions, on timescales relevant to the in vivo processes in bacterial membranes. In contrast, during our SMFS experiments the tip–sample contact time is in the range 2–4 ms and the repetition rate is 1 Hz.

The degradation of cyanide, however, remained relatively constant with AZD2281 cell line further increase in the reaction time beyond 180 min, indicating that the catalyst might be deactivated by deposition of the reaction products on the catalyst surface. Figure 7 Photocatalytic degradation

of cyanide using different concentration wt.% of calcined ZnO E . Reaction conditions: 100 ppm KCN(aq), t = 25°C, pH = 8.5. Kinetic photocatalytic degradation of CN- using calcined ZnOE The first order kinetic degradation of CN – (aq) was fitted to the following expression: where [C]t and [C]o represent the concentration in (ppm) of CN¯ (aq) in solution at time zero and at time t of illumination, respectively, and k represents the apparent rate constant (min-1). The kinetic analysis of cyanide photodegradation is depicted in Figure  8, which shows that the rate of photocatalytic reaction depends on the concentration of the catalyst. An excellent correlation to

the pseudo-first-order reaction kinetics (R > 0.99) was found. Obviously, the photodegradation rate of the CN- was found to increase from 19.2 to 42.9 × 10-3 min-1 with increasing ZnO loading from 0.01 to 0.07 wt.% (Table  5). Figure 8 Photodegradation kinetic of cyanide ion over calcined ZnO E . Table 5 Apparent rate constant ( k ) at different concentration wt.% of calcined ZnO E ZnOEconcentration, wt.% k(min × 10-3) 0.01 19.2 0.02 20.8 0.03 33.5 0.05 36.1 0.07 42.9 Conclusion Zinc oxide nanoparticles Selleckchem R788 were readily prepared at room

temperature from zinc nitrate Cell press hexahydrate and cyclohexylamine either in aqueous or ethanolic medium. The calcined ZnOE had a regular, polyhedra morphology while the calcined ZnOW had irregular spherical morphology, mixed with some chunky particles. The morphology was a key factor in the superior photocatalytic behavior of ZnOE over that of ZnOW. The differences in morphology and photocatalytic behavior are strongly influenced by the physicochemical properties of the synthesis medium. Acknowledgements The authors gratefully thank King Abdulaziz City for Science and Technology (KACST) for financing this work through project No. 29–280. We also thank Dr. Mohamad Mokhtar and Reda Mohammed for their useful discussion, Mr. Emad Addurihem for his technical assistance, Mr. Abdulrahman AL-Ghihab for SEM analysis, and Mr. Muath Ababtain for TEM analysis. References 1. Mudder TI, Botz MM: Cyanide and society: a critical review. Eur J Miner Process Environ Protect 2004, 4:62–74. 2. Young CA: Remediation of technologies for the management of aqueous cyanide species . In Cyanide: Social, Industrial and Economic Aspects. Edited by: Young CA, Tidwell LG, Anderson CG. Warrendale, PA: TMS; 2001:175–194. 3. Zagury GJ, Oudjehani K, Deschenes L: Characterization and variability of cyanide in solid mine tailings from gold extraction plants.

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36. Stevens MP, Stevens JM, Jeng RL, Taylor LA, Wood GSK3235025 concentration MW, Hawes P, Monaghan P, Welch MD, Galyov EE: Identification of a bacterial factor required for actin-based motility of Burkholderia pseudomallei. Mol Microbiol 2005, 56(1):40–53.PubMedCrossRef 37. Hertweck C: The biosynthetic logic of polyketide diversity. Angew Chem Int Ed Engl 2009, 48(26):4688–4716.PubMedCrossRef 38. Darwin KH, Miller VL: Type III secretion chaperone-dependent regulation: activation of virulence genes by SicA and InvF in Salmonella typhimurium. EMBO J 2001, 20(8):1850–1862.PubMedCentralPubMedCrossRef 39. Kane CD, Schuch R, Day WA Jr, Maurelli AT: Gemcitabine ic50 MxiE regulates

intracellular expression of factors secreted by the Shigella flexneri 2a type III secretion system. J Bacteriol 2002, 184(16):4409–4419.PubMedCentralPubMedCrossRef 40. Walker KA, Miller VL: Regulation of the Ysa type III secretion system of Yersinia enterocolitica by YsaE/SycB and YsrS/YsrR. J Bacteriol 2004, 186(13):4056–4066.PubMedCentralPubMedCrossRef 41. Deane JE, Abrusci P, Johnson S, Lea SM: Timing is everything: the regulation of type III secretion. Cell Mol Life Sci 2010, 67(7):1065–1075.PubMedCentralPubMedCrossRef 42. Tucker SC, Galan JE: Complex function for SicA, a Salmonella enterica serovar typhimurium type III secretion-associated chaperone. J Bacteriol 2000, 182(8):2262–2268.PubMedCentralPubMedCrossRef 43. Parsot C, Ageron E, Penno Dapagliflozin C, Mavris M, Jamoussi K, d’Hauteville H, Sansonetti P, Demers B: A secreted anti-activator, OspD1, and its chaperone,

Spa15, are involved in the control of transcription by the type III secretion apparatus activity in Shigella flexneri. Mol Microbiol 2005, 56(6):1627–1635.PubMedCrossRef 44. Tuanyok A, Auerbach RK, Brettin TS, Bruce DC, Munk AC, Detter JC, Pearson T, Hornstra H, Sermswan RW, Wuthiekanun V, Peacock SJ, Currie BJ, Keim P, Wagner DM: A horizontal gene transfer event defines two distinct groups within Burkholderia pseudomallei that have dissimilar geographic distributions. J Bacteriol 2007, 189(24):9044–9049.PubMedCentralPubMedCrossRef 45. Biggins JB, Ternei MA, Brady SF: Malleilactone, a polyketide synthase-derived virulence factor encoded by the cryptic secondary metabolome of Burkholderia pseudomallei group pathogens. J Am Chem Soc 2012, 134(32):13192–13195.PubMedCentralPubMedCrossRef 46. Lamont IL, Beare PA, Ochsner U, Vasil AI, Vasil ML: Siderophore-mediated signaling regulates virulence factor production in Pseudomonasaeruginosa.

The animals were housed in an air-conditioned room (21–24 °C) under 12 h of light (7:00–19:00) and were allowed free access to food pellets and water throughout the study. Animal experiments Female mice were anesthetized with sodium pentobarbital (40 mg/kg, i.p.) for see more the bilateral removal of the ovaries. The mice in the sham-operated group were anesthetized, laparotomized, and sutured without removal of the ovaries. After 3 days of recovery from surgery, the OVX mice were randomly divided into four groups and orally treated with

vehicle (H2O), kinsenoside (100 and 300 mg/kg daily), or alendronate (2.5 mg/kg every other day; Sigma-Aldrich, St. Louis, MO, USA) for 4 weeks. The sham-operated group was orally treated with H2O only. Plasma ALP levels were measured using clinical kits (Roche Diagnostics, Mannheim, Germany) and a spectrophotometric system (Cobas Mira; Roche, Rotkreuz, Switzerland). Plasma CTx levels were determined using a mouse-specific enzyme-linked immunosorbent assay (ELISA) according to the manufacturer’s protocols (Nordic Bioscience Diagnostics, Herlev Hovedgade, Denmark). Microtomography analysis was performed as reported previously [20]. The trabecular bone microarchitecture of the distal right femoral metaphysis was measured using a microtomography scanner (SkyScan

1076, Kontizh, Belgium), with Ku 0059436 an isotropic resolution of 18 μm in all three spatial dimensions. Acetophenone Bone volume and tissue volume were measured directly from the original three-dimensional images, and trabecular bone volume (bone volume/tissue volume, percent) was calculated by dividing the bone volume by the total volume of interest. Other parameters of trabecular structure were studied, including thickness, separation, and the number of trabeculae, as calculated directly from three-dimensional images. The left femur was removed, fixed with 4 % neutral-buffered paraformaldehyde in phosphate-buffered saline

(PBS; pH 7.4) for 48 h, and decalcified in 10 % ethylenediamine tetraacetic acid solution (pH 7.4) at 4 °C for 4 weeks. After decalcification, each bone sample was cut along the coronal plane, embedded in paraffin, and cut longitudinally into sections for histological staining. For measurement of the osteoclast number, sections were stained for tartrate-resistant acid phosphatase (TRAP) with TRAP kit (Sigma-Aldrich, St. Louis, MO, USA) as previously described [21]. To explore the mechanisms associated with kinsenoside on OVX-induced osteoporosis in mice, total RNA of the right tibiae was extracted for analysis of RT-PCR. The expression levels of ALP, matrix metalloproteinase-9 (MMP-9), and TRAP were normalized to that of GAPDH mRNA in the same tissue. The PCR products were separated on a 2 % agarose gel and recorded on Polaroid film; the band was quantified with a densitometer.

“
“Background Helicobacter pylori is carried by more than half of the world’s adult population [1]. It can chronically colonize the human gastric mucosa, where it is found in the mucus layer and is adhered to epithelial cells [2]. Although most infected subjects remain asymptomatic, infection with H. pylori can promote severe gastritis [3] and significantly increase the risk of gastric malignancies [4, 5]. In some epidemiological studies, H. pylori eradication was shown to be effective in gastric cancer prevention [6, 7]. Additionally, H. pylori BAY 73-4506 purchase eradication was found to decrease the incidence and the severity of lesions with carcinogenic potential in animal

models [8, 9]. Natural mechanisms that protect the host from H. pylori infections depend on the function of the innate defense system in which antibacterial peptides such as cathelicidin LL-37 [10, 11] and O-glycans in gastric mucin [12] play a key role. LL-37 find more is a proteolytically processed peptide derived from the C-terminal domain of human cathelicidin (hCAP-18/LL-37) that is constitutively released to the extracellular space by phagocytic

granulocytes and epithelial cells [13]. Functions ascribed to LL-37 include prevention of bacterial growth [14], neutralization of bacterial wall molecule bioactivity [15], and activation of host cells by binding specific cell membrane receptors [16–18]. H. pylori upregulates the production of LL-37/hCAP18 by the gastric epithelium, suggesting that cathelicidin or its derivative LL-37 contributes to determining the balance between host mucosal defense and H. pylori survival mechanisms that govern chronic infection with this gastric pathogen [10, 11]. Cationic antibacterial peptides (CAPs) including LL-37 have been extensively investigated as a potential source of new antibacterial molecules. The engineered WLBU2 peptide whose residues are Calpain arranged to form an amphipathic helical structure with optimal charge and hydrophobic density, overcomes some limitations of natural LL-37 such as sensitivity to Mg2+ or Ca2+ and inactivation by blood serum [19]. Therefore

WLBU2 could treat infections where LL-37 is ineffective. In order to generate molecules able to mimic CAPs’ ability to compromise bacterial membrane integrity, non-peptide ceragenins with cationic, facially amphiphilic structures characteristic of most antimicrobial peptides were developed. Ceragenins such as CSA-13 reproduce the required CAP morphology using a bile-acid scaffolding and appended amine groups [20]. They are bactericidal against both Gram-positive and Gram-negative organisms, including drug-resistant bacteria such as clinically relevant methicillin-resistant Staphylococcus aureus (MRSA), and a previous susceptibility study demonstrated that CSA-13 has a MIC50/MBC50 ratio of 1 [21, 22]. In this study we compare the bactericidal potency of LL-37, WLBU2 and CSA-13 against clinical isolates of H. pylori.

ichthiosmia CECT 4486T 132 – - 122 104 116 110 81 19 102 Environment, Surface water

– NA, Germany, 1986   A. veronii CECT 7059 164 – - 151 133 145 138 33 109 39 Environment, Drinking water – Zaragoza, Spain, 2002 A. caviae (n=34) BVH16 9 1 B 9 8 9 9 3 8 8 Human, Respiratory tract C Rambouillet, Fr, 2006   BVH57 43 1 B 43 8 9 9 3 32 8 Human, Blood I Versailles, Fr, 2006   BVH63 47 6 F 12 10 43 41 3 10 41 Human, www.selleckchem.com/Akt.html Blood I Macon, Fr, 2006   BVH84 47 6 F 12 10 43 41 3 10

41 Human, Stool I Aix en Provence, Fr, 2006   BVH98 72 – F 12 10 64 60 37 10 41 Human, Wound I Brest, Fr, NA   ADV118 79 6 F 72 10 43 8 3 10 41 Human, Wound I Montpellier, Fr, 2009   ADV121 81 – F 74 10 43 8 3 3 63 Human, Stool ND Montpellier, Fr, 2009   BVH48 34 2 C 34 10 32 32 27 26 32 Human, Vagina C Monceau les mines, Fr, 2006   A. caviae CCUG 48892 175 2 C 34 10 32 32 27 3 32 Environment, Water   Uppsala, Sweden, 2004   BVH19 11 – C 11 10 3 11 3 10 10 Human, Vagina C Villeneuve sur Lot, Fr, 2006   BVH81 61 – C 34 10 3 11 3 26 32 Human, Stool C Aix en Provence, Fr, XL184 order 2006   BVH66 50 – C 34 10 46 44 37 26 32 Human, Wound I Martinique Island, Fr, 2006   BVH55 41 3 C 41 10 39 12 3 26 32 Human, Stool I Saint-Denis, Fr, 2006   BVH87 64 3 C 59 10 39 12 3 26 32 Human, Stool I Aix en Provence, Fr, 2006   BVH4 3 – - 3 3 3 3 3 3 3 Human, Wound I Cahors, Fr, 2006

  BVH15 8 – - 8 7 8 8 6 7 7 Human, Blood I Grasse, Fr, 2006   BVH20 12 – - 12 10 11 12 3 8 11 Human, 17-DMAG (Alvespimycin) HCl Stool I Gonesse, Fr, 2006   BVH51 37 – - 37 32 35 35 29 28 35 Human, Blood I Monaco, Fr, 2006   BVH52 38 – - 38 33 36 36 30 29 36 Human, Blood I Monaco, Fr, 2006   BVH67 51 – - 49 32 47 45 3 8 35 Human, Stool ND Martinique Island, Fr, NA   BVH85 62 – - 57 48 55 11 3 40 8 Human, Stool I Aix en Provence, Fr, 2006   BVH86 63 – - 58 49 56 53 43 41 51 Human, Stool C Aix en Provence, Fr, 2006   BVH100 73 – - 67 56 65 61 50 26 58 Human, Wound ND Brest, Fr, ND   ADV106 77 – - 70 59 68 64 52 50 35 Human, Stool ND Montpellier, Fr, 2008   ADV124 82 – - 75 62 71 67 3 53 64 Human, Stool ND Montpellier, Fr, 2009   AK223 98 – - 91 74 86 81 3 8 77 Environment, Waste water treatment lagoon – Montracol, Fr, 2006   AK229 101 – - 34 77 89 84 37 3 78 Environment, Waste water treatment lagoon – Montracol, Fr, 2006   AK231 102 – - 94 78 90 85 63 26 32 Environment, Waste water treatment lagoon – Montracol, Fr, 2006   AK234 104 – - 96 10 92 87 65 66 80 Environment, Waste water treatment lagoon – Montracol, Fr, 2006   AK245 115 – - 105 88 100 11 70 71 88 Environment, Water lake – Annecy, Fr, 1998   A.