78-fold) and AQY1 (aquaporin water channel, up-regulated by 2.73-fold), which all belong to the group of C. neoformans genes regulated by osmotic stress [49]. It is possible that defects in the plasma membrane resulting from inhibition of ergosterol biosynthesis

Eltanexor by FLC affects transport of small molecules through the membrane. Analysis of the H99 genome sequence [16] predicted 54 ATP-Binding Cassette (ABC) transporters and 159 major facilitator superfamily (MFS) transporters, suggesting wide transport capabilities of this environmental yeast [50]. However, we found only two S. cerevisiae transporter homologues with significant increased expression. One is PDR15 that is a member of the ABC transporter subfamily exporting antifungals and other xenobiotics in fungi [51]. The other gene

is Selleckchem PD0332991 ATR1 that encodes a multidrug resistance transport protein belonging to the MFS class of transporters. ATR1 expression was recently shown to be upregulated by boron and several stress conditions [52]. To date, Afr1 (encoded by AFR1; also termed CneAfr1) and CneMdr1 are the only two efflux pumps associated with antifungal drug resistance in C. neoformans [50]. Since Afr1 is the major efflux pump mediating azole resistance in C. neoformans [11, 15], the absence of altered AFR1 expression could be expected. Not surprisingly, we Oxymatrine noticed downregulated expression (2.35-fold) of FLR1 (for fluconazole resistance) encoding a known MFS multidrug transporter in yeast, that is able to confer resistance to a wide range of dissimilar drugs and other

chemicals [53]. This may suggest that both AFR1 and FLR1 do not participate to the short-term stress induced by FLC in C. neoformans. Effect of FLC on the susceptibility to cell wall inhibitors It was demonstrated that compounds interfering with normal cell wall formation (Congo red, calcofluor white, SDS and caffeine) affect growth of C. neoformans strains with altered cell wall integrity [27]. For instance, several deletion strains for genes involved in the PKC1 signal transduction pathway were found to be sensitive to SDS and Congo red and to a lesser extent caffeine. To test the hypothesis that FLC treatment might induce cell wall stress, we analyzed H99 cells for susceptibility to the cell wall perturbing agents, before and after the cells were exposed for 90 min to FLC at sub-MIC concentration (10 mg/l) at 30°C. Phenotypes of H99 cells on cell wall inhibitor plates are shown in Figure 3. The FLC pre-treated H99 cells were slightly more resistant to all four cell wall inhibitors as compared to untreated cells. These findings are consistent with expression changes of cell wall associated genes identified in our microarray analysis.

B. Schematic of VPI-2 excision mechanism and primer pair VPI2attF and VPI2attR used to detect the VPI-2 attB locus after excision of the entire region. VPI-1 and VPI-2 do

not share any genes in common but do share some functional characteristics such as the ability selleck kinase inhibitor to integrate into the chromosome, specifically at a tRNA site using an integrase belonging to the tyrosine recombinase family [16, 18, 23, 26, 28]. VPI-2 integrates into chromosome 1 at a tRNA-serine locus, whereas VPI-1 is located at the tmRNA locus. Both regions are flanked by direct repeats (DRs) named attL and attR [16, 18, 23, 26, 28]. These integrases, IntV1 (VC0847) and IntV2 (VC1758), are believed to mediate insertion into the host chromosome through site specific recombination between an attachment site attP, present in the pathogenicity island, and attB, present in the bacterial chromosome. Pathogenicity islands have been shown to excise from their host genome in pathogenic Escherichia coli and Yersinia species [29–36]. In E.

coli strain 536, a uropathogenic isolate, Hacker and colleagues have identified six PAIs, all of which encode a tyrosine recombinase integrase and are flanked by DRs [31, 33, 36–39]. They demonstrated that PAI-I, II, III and V can excise from the chromosome by site-specific recombination involving selleckchem their respective DRs (attL and attR) [31, 33]. The PAIs were shown to excise at different frequencies depending on the growth conditions [31, 33]. Likewise, both VPI-1 and VPI-2 have been shown to excise from their host chromosome [23, 28]. Rajanna and colleagues demonstrated that VPI-1 can

excise from V. cholerae N16961 at very low rates [28]. They determined that the integrase IntV1 (VC0847) was not essential for excision since a transposase within the region appeared to compensate for an IntV1 knockout [28]. Recently, Murphy and Boyd demonstrated that VPI-2 from V. cholerae N16961 can excise from chromosome 1, which also occurred at very low frequency under optimal growth conditions [23]. Their study showed that IntV2 (VC1758) was essential for excision and the formation of a circular click here intermediate (CI) [23]. Pathogenicity islands from both E. coli and V. cholerae are non-self mobilizable, they do not encode any proteins such as those for phage structural proteins or conjugation systems needed for cell to cell mobility [23, 28, 31, 33, 36–39]. The mechanism of transfer for most pathogenicity islands remains to be elucidated but likely involves hitchhiking with plasmids, conjugative transposons, Integrative and Conjugative Elements (ICEs), or generalized transducing phages or uptake by transformation. It is known that for some mobile and integrative genetic elements (MIGEs) the presence of a recombination directionality factor (RDF)/excisionase is required for excision [40, 41]. For instance, Xis is required for the excision of the ICE SXT from V.

It also appears that analysis with specialized tools, organized on a “”one feature at a time”" basis (Lipo SPs, TAT

SPs …), most reliably gives predictions consistent with experimental data. For this purpose, CoBaltDB is a unique and innovative resource. 2-Using CoBaltDB to analyse protein(s) and a proteome One valuable property of CoBaldDB is to recapitulate all pre-computed predictions in a unique A4-formated synopsis. This summary is very helpful for assessing computational data such as the variation and frequency in the predictions of signal peptide cleavage sites: such predictions are sometimes significantly consistent, but often Bioactive Compound Library price SN-38 purchase are not in agreement with each other (Figure 7A). However, correct identification of signal peptide cleavage sites is essential in many situations, especially for producing secreted recombinant proteins. Figure 7 Using CoBaltDB to analyse protein(s) and a proteome. A: Comparative analysis of SP cleavage site predictions (proteinssecreted by P. aeruginosa); B: Discriminating between SPI- and SP II cleavage sites. The CoBaltDB synopsis could also be used to discriminate between SignalPeptidaseII- and SignalPeptidaseI-cleaved signals and between SPs and N-terminal

transmembrane helices. Indeed, most localization predictors have difficulties distinguishing between type I

and type II signal peptidase cleavages. CoBaltDB can be exploited in an interesting way to benchmark this prediction by displaying all cleavage site predictions Methamphetamine in a “”decreasing sensitivity”" arrangement (SpII then Tat-dependant SPI then Sec-SPI). By considering lipoprotein datasets from different organisms, we evidenced two principal profiles (Figure 7B) and found that all experimentally validated lipoproteins score 100% (all tools give the same prediction) or 66% in the CoBaltDB LIPO column (see explanation in the paragraph above). In addition, in almost all of the examined cases, tools dedicated to Twin-arginine SP detection do not identify SpII-dependent SP, whereas the Sec-SP predictors detect both Sec and Tat-type I as well as type II signal-anchor sequences. These observations allow us to propose, for our data set, thresholds for each box: as previously illustrated, lipoproteins have score > 66% in the LIPO prediction box; Tat-secreted proteins have 0% in the LIPO box and 100% for the two TAT-dedicated tools; Sec-secreted proteins have 33% in the LIPO Box (due to the fact that LipoP detects both SpI and SpII [59]), 0% in the TAT-tools, and > 80% in SEC-specialized tools. Rules of this type can be used to check entire proteomes for evaluation of the different secretomes as illustrated in the following case studies.

New J Phys 2010, 12:013020.CrossRef 7. Coey JMD, Venkatesan M, Fitzgerald CB: Donor impurity band exchange in dilute ferromagnetic oxides. Nat Mater 2005, 4:173–179.CrossRef 8. Belghazi Y, Schmerber G, Colis S, Rehspringer JL, Dinia A, Berrada A: Extrinsic origin of ferromagnetism in ZnO and Zn 0.9 Co 0.1 O magnetic semiconductor PRI-724 mouse films prepared by sol-gel technique. Appl Phys Lett 2006, 89:122504.CrossRef 9. Samanta K, Bhattacharya P, Katiyar RS: Optical properties of Zn 1-x Co x O thin

films grown on Al 2 O 3 (0001) substrates. Appl Phys Lett 2005, 87:101903.CrossRef 10. Dinia A, Schmerber G, Mény C, Pierron-Bohnes V, Beaurepaire E: Room-temperature ferromagnetism in Zn 1-x Co x O magnetic semiconductors prepared by sputtering. J Appl Phys 2005, 97:123908.CrossRef 11. Lee H-J,

Park CH, Jeong S-Y, Yee K-J, Cho CR, Jung M-H, Chadi DJ: Hydrogen-induced ferromagnetism in ZnCoO. Appl Phys Lett 2006, 88:062504.CrossRef 12. Lee mTOR inhibitor H-J, Choi SH, Cho CR, Kim HK, Jeong S-Y: The formation of precipitates in the ZnCoO system. Europhys Lett 2005, 72:76–82.CrossRef 13. Lee S, Cho YC, Kim S-J, Cho CR, Jeong S-Y, Kim SJ, Kim JP, Choi YN, Sur JM: Reproducible manipulation of spin ordering in ZnCoO nanocrystals by hydrogen mediation. Appl Phys Lett 2009, 94:212507.CrossRef 14. Kim SJ, Cha SY, Kim JY, Shin JM, Cho YC, Lee S, Kim W-K, Jeong S-Y, Yang YS, Cho MycoClean Mycoplasma Removal Kit CR, Choi HW, Jung MH, Jun B-E, Kwon K-Y, Kuroiwa Y, Moriyoshi C: Ferromagnetism in ZnCoO due to hydrogen-mediated Co–H–Co complexes: how to avoid the formation

of Co metal clusters? J Phys Chem C 2012, 116:12196–12202.CrossRef 15. Lee S, Kim B-S, Cho YC, Shin J-M, Seo S-W, Cho CR, Takeuchi I, Jeong S-Y: Origin of the ferromagnetism in ZnCoO from chemical reaction of Co 3 O 4 . Curr Appl Phys 2013, 13:2005–2009.CrossRef 16. Cho YC, Kim S-J, Lee S, Kim SJ, Cho CR, Nahm H-H, Park CH, Jeong IK, Park S, Hong TE, Kuroda S, Jeong S-Y: Reversible ferromagnetism spin ordering governed by hydrogen in Co-doped ZnO semiconductor. Appl Phys Lett 2009, 95:172514.CrossRef 17. Cho YC, Lee S, Nahm HH, Kim SJ, Park CH, Lee SY, Kim S-K, Cho CR, Koinuma H, Jeong S-Y: Conductive and ferromagnetic contributions of H in ZnCoO using H 2 hot isostatic pressure. Appl Phys Lett 2012, 100:112403.CrossRef 18. Li L, Guo Y, Cui XY, Zheng R, Ohtani K, Kong C, Ceguerra AV, Moody MP, Ye JD, Tan HH, Jagadish C, Liu H, Stampfl C, Ohno H, Ringer SP, Matsukura F: Magnetism of Co-doped ZnO epitaxially grown on a ZnO substrate. Phys Rev B 2012, 85:174430.CrossRef 19. Kim SJ, Lee S, Cho YC, Choi YN, Park S, Jeong IK, Kuroiwa Y, Moriyoshi C, Jeong S-Y: Direct observation of deuterium in ferromagnetic Zn 0.9 Co 0.1 O:D. Phys Rev B 2010, 81:212408.CrossRef 20.

(#) CDRPMI, (##) CDM-C16alone. The profound growth arrest of P. falciparum was investigated further by culturing parasites synchronized at the ring stage in CDM containing different concentrations of C16:0, which was added individually, for 28 h. Suppression of schizogony, particularly the progression of the parasite to the trophozoite stage following the ring stage, was detected in CDM containing C16:0 alone as the NEFA growth factor, regardless of a wide range of concentrations (Figure  8).

On the other hand, all stages of parasites cultured in CDRPMI had comparable development to those ITF2357 price cultured in GFSRPMI (Figure  8). This implies that C18:1 protected the parasite completely from C16:0-induced growth arrest. Figure 8 Modification of P. falciparum development in CDMs containing C16:0 only as a NEFA growth factor. Synchronized parasites at the ring stage were cultured in CDM containing graded concentrations of C16:0 (C16:0–20, 20 μM; C16:0–60, 60 μM; C16:0–160, 160 μM) for 28 h. Each developmental stage was counted after Giemsa staining. Levels of parasitemia were 5.27 ± 0.08 (GFSRPMI), 5.27 ± 0.34 (CDRPMI), 3.61 ± 0.30 (C16:0–20), 3.69 ± 0.60 (C16:0–60), and 3.67 ± (C16:0–160); Caspase inhibitor (*) indicates CDM-C16alone. The morphology of the rings observed in the presence of C16:0 and the schizonts in GFSRPMI and CDRPMI is shown. Although profound growth arrest was detected

in P. falciparum cultured in CDM containing C18:1 alone for a longer period (95 h), all stages of the parasite cultured for 28 h had comparable development to those cultured in CDRPMI and GFSRPMI. However the majority of merozoites were incomplete, resulting in a low growth rate during the longer culture period (Figure  7). Thus, the growth arrest associated with CDM containing C18:1 alone did not involve suppression of schizogony. Developmental C1GALT1 arrest of P. falciparum was detected at the early stage in CDM-C16alone, similar to that with CDRPMI and

GFSRPMI in the presence of Neocuproine and TTM, which cause perturbation of copper homeostasis. We have predicted previously, using genome-wide transcriptome profiling, five transcripts associated with the blockage of trophozoite progression from the ring stage [7], of which one transcript was a putative copper channel (PF3D7_1421900 at PlasmoDB [6]). This suggests a critical function of copper ions and copper-binding proteins in the early developmental arrest of the parasite, in agreement with the results with Neocuproine and TTM. Genes encoding proteins that are involved in the copper pathway and trafficking in various microbes have been identified in P. falciparum. These proteins include: 1) a putative copper channel (XP_001348385 at NCBI), 2) a copper transporter (XP_001348543.1 at NCBI), 3) a putative COX17 (XP_001347536 at NCBI), and 4) a copper-transporting ATPase (XP_001351923 at NCBI).

J Biol Chem 2004, 279:9064–9071.PubMedCrossRef 32. Mellies JL, Haack KR, Galligan DC: SOS regulation of the type III secretion system of enteropathogenic Escherichia coli . J Bacteriol 2007, 189:2863–2872.PubMedCrossRef 33. Justice SS, Hung C, Theriot JA, Fletcher

DA, Anderson GG, Footer MJ, Hultgren SJ: Differentiation and developmental pathways of uropathogenic Escherichia coli in urinary tract pathogenesis. Proc Natl Acad Sci USA 2004, 101:1333–1338.PubMedCrossRef 34. Dörr T, Lewis K, Vulić M: SOS response induces persistence to fluoroquinolones in Escherichia coli . PLoS Genetics 2009, 5:1–9.CrossRef 35. Keseler IM, Bonavides-Martinez C, Collado-Vides J, Gama-Castro S, Gunsalus RP, Johnson DA, Krummenacker M, Nolan LM, Paley S, Paulsen IT, et al.: EcoCyc: a comprehensive view of Escherichia coli biology. Nucleic Acids BLZ945 in vitro Res 2009, 37:D464–470.PubMedCrossRef 36. Salles B, Weisemann JM, Weinstock GM: Temporal control of colicin E1 induction.

J Bacteriol 1987, 169:5028–5034.PubMed selleck compound 37. Salles B, Weinstock GM: Interaction of the CRP-cAMP complex with the cea regulatory region. Mol Gen Genet 1989, 215:537–542.PubMedCrossRef 38. Chant EL, Summers DK: Indole signaling contributes to the stable maintenance of Escherichia coli multicopy plasmids. Mol Microbiol 2007, 63:35–43.PubMedCrossRef Authors’ contributions SK performed all experiments. ZP contributed to analysis of the results. OG and DŽB participated in the design of the experiments and SK, OG and DŽB in preparation of the manuscript. All authors read and approved the final manuscript.”
“Background Nitrogen-fixing symbiotic bacteria, commonly known as rhizobia, employ a variety of strategies which allow them to exist in the soil and adapt to various environmental conditions

prior to infecting leguminous plant hosts. Rhizobial cell surface components, exopolysaccharide (EPS) and lipopolysaccharide (LPS), play an important role in determining the symbiotic competence of rhizobia, root tissue invasion and induction of nitrogen-fixing nodules on host plants forming indeterminate-type nodules, such as Pisum, Trifolium, Vicia, and Medicago spp. [1–4]. Acidic EPSs secreted in large amounts by rhizobia aminophylline are species-specific compounds consisting of common sugars substituted with non-carbohydrate residues [1, 4–6]. EPS of Rhizobium leguminosarum is a heteropolymer consisting of octasaccharide subunits composed of five glucose residues, one galactose, and two glucuronic acid residues, additionally decorated with acetyl, pyruvyl, and 3-hydroxybutyryl groups [7, 8]. EPS-deficient mutants or those with an altered LPS structure are impaired in nodule cell invasion and nitrogen fixation [1, 6, 9–11]. Biosynthesis of EPS in R. leguminosarum is a multi-step process requiring the expression of several pss genes, located in the major EPS cluster on the chromosome [12, 13].

The arrows indicated sampling. (C) Gene expression of SPG1598, SPG1592, and SPG1591 in medium supplemented with amino sugars are compared to growth in glucose. Variation of gene expression is shown for genes of bacteria grown in ManNAc (open bars), glucose plus ManNAc (open striped bars), NeuNAc (grey bars), and glucose plus NeuNAc (grey striped bars). Results are represented

as fold changes ± SD of gene expression from 3 to 4 independent experiments. Statistical analysis was carried out using Tukey’s Multiple Comparison Test (ns non significant; *, p < 0.05; **, p < 0.01). Generation time on glucose containing media is 38–45 min, 90 min on NeuNAc and 140 min on ManNAc. Repression of the nanAB locus in the presence of glucose According to the

Belinostat mw presence of three cre sites within the pneumococcal neuraminidase locus, we observed a biphasic growth curve when bacteria grew on glucose plus ManNAc or NeuNAc (Figure 4A,B, open squares). To demonstrate that this phenotype was due to carbon catabolite repression, we investigated the transcriptional behaviour of the neuraminidase locus in the presence or absence of glucose in the medium. Growth Semaxanib molecular weight conditions used were as follows: ManNAc with and without glucose (Figure 4A, open triangles and open squares), NeuNAc with and without glucose (Figure 4B, open triangles and open diamonds) and glucose as the sole carbon source as a reference condition (Figure 4A and 4B, closed circles). Growth curve data show that addition of glucose to both ManNAc and NeuNAc resulted in an initial growth on glucose as a preferred carbon source followed by a second slower growth phase, in which the amino sugars were metabolised. To assess glucose repression during growth on glucose gene expression analysis was carried out by sampling the bacteria at an OD590 of 0.05 (Figure 4A,B, arrows). As shown in Figure 4C, the over-expression of all genes of Prostatic acid phosphatase the nanAB locus occurred during growth on ManNAc or NeuNAc as the sole carbon sources (Figure 4C, open and grey bars), while it was completely repressed in the presence of glucose (Figure 4C, striped bars). Regulation of neuraminidase

A production and activity by ManNAc To assess the production of NanA on the bacterial surface after induction of the nanAB locus by ManNAc or NeuNAc, we performed a cytofluorimetry assay. In these experiments bacteria were harvested at the late exponential phase. In this assay the anti-NanA serum recognises also to a certain extent glucose grown bacteria (Figure 5A). However in culture media with either ManNAc or NeuNAc as the sole carbon sources, the number of NanA expressing bacterial cells significantly increased reaching 73.7% (± 3.4) and 79.6% (± 4.9), respectively. Differences in NanA production between bacterial cells grown with either of the two amino sugars and control cells cultured in glucose or glucose plus ManNAc were statistically significant (Figure 5A).

CD44 is a key receptor for hyaluronan, critical for cell signalling and drug resistance. We investigated the expression of CD147, CD44, and transporter (MDR1) and MCT proteins in CaP progression. Methods: CD147, CD44s and v3-10, MDR1, MCT1 and MCT4 expression was studied in human metastatic CaP cell lines (PC-3 M-luc(MDR), PC-3 M-luc, Du145, LN3, 4SC-202 DuCaP) and primary CaP tumours, lymph node metastases and normal prostate, using immunoperoxidase, immunofluorescence and microscopy. Cell line dose-response and sensitivity (IC50) to docetaxel was measured with

MTT, and correlated with CD147, CD44, MDR1, and MCT expression. Results: PC-3 M-luc (MDR), PC-3 M-luc and Du145 cells expressed high level CD147, CD44, MDR1 and MCT. In contrast, DuCaP cells showed no CD147 or CD44, but weak MCT immunostaining. LN3 cells expressed

strong CD147 and MCT, weak CD44v and MDR1, and no CD44s. Docetaxel sensitivity was positively related to CD44, CD147, MDR1 and MCT expression. Strong heterogeneous CD147, CD44, MDR1, MCT expression was found in high grade primary tumours (Gleason score >7). Heterogeneous co-localization of CD147 with CD44, MDR1 and MCT was found in PC-3 and Du145 cells, and in high grade tumours. Conclusions: Metastatic CaP cell lines and primary CaP displayed overxpression of CD147, CD44, MDR1, MCT proteins. Interactions between learn more these proteins could contribute to the development of CaP drug resistance and metastasis. Selective targeting of CD147 and CD44 to block their activity (alone or combined) may limit tumour metastasis, and increase drug sensitivity by modifying expression of MDR and MCT proteins. Poster No. 185 Metallic Ion Composition Discriminates between Normal Esophagus, Dysplasia, and Carcinoma Daniel Lindner 1 , Derek Raghavan1, Michael Kalafatis3, Charis Eng2, Gary Falk4 1 Taussig Cancer Institute, Cleveland Clinic, Cleveland, OH, USA, 2 Genomic Medicine Institute, Cleveland Clinic, Cleveland, OH, USA, 3 Department of Chemistry, Cleveland State University, Cleveland, OH, USA,

4 Digestive Disease Institute, Cleveland Clinic, Cleveland, OH, USA Subtractive hybridization, and more recently, whole genome expression arrays 4-Aminobutyrate aminotransferase have advanced our understanding of differential gene expression in neoplastic compared to normal tissues, leading to identification of several important oncogenes as well as tumor suppressor genes. We hypothesized that such changes in gene expression would not only result in differential protein expression profiles, but would also ultimately result in detectable differences in the ionic composition of normal, dysplastic, and neoplastic tissues. In a blinded fashion, we utilized atomic absorption (AA) to analyze the metallic ion composition (iron, zinc, copper, chromium, magnesium, and manganese) in normal human esophagus, low grade dysplasia, intestinal metaplasia (Barrett’s esophagus), high grade dysplasia, and carcinoma.

PubMedCrossRef 44. Vidal JE, Navarro-Garcia F: EspC translocation into epithelial cells by enteropathogenic Escherichia coli requires a concerted participation of type V and III secretion systems. Cell Microbiol 2008,10(10):1975–1986.PubMedCrossRef 45. Greco R, De Martino L, Donnarumma G, Conte MP, Seganti L, Valenti P: Invasion of cultured human cells by

Streptococcus pyogenes. Res Microbiol 1995,146(7):551–560.PubMedCrossRef 46. Prasad KN, Dhole TN, Ayyagari A: Adherence, invasion and cytotoxin assay of Campylobacter jejuni in HeLa and HEp-2 cells. J Diarrhoeal Dis Res 1996,14(4):255–259.PubMed 47. Baumler AJ, Tsolis RM, Heffron F: Contribution of fimbrial selleck inhibitor operons to attachment to and invasion of epithelial cell lines by Salmonella typhimurium. Infect Immun 1996,64(5):1862–1865.PubMed Competing interests The authors declare that they have no competing interests. Authors’ contributions JZ performed the molecular genetic studies, participated in sequence analysis,

constructed the pic gene deletion mutant and pic gene complementation AZD2171 strains, carried out mouse Sereny tests and drafted the manuscript. XC participated in mouse Sereny tests and conducted H&E staining. XL conducted mPCR tests and performed HeLa cell gentamicin protection assays. LQ and YW participated in the design of the study, performed statistical analysis and edited the manuscript. DQ and YW participated in the design and coordination of the study, and helped to draft and edit the manuscript. All authors read and approved the final version of the manuscript.”
“Background Hfq is an RNA chaperone broadly implicated in sRNA function in many bacteria. Hfq interacts with and stabilizes many sRNAs, and it is thought to help promote sRNA-mRNA target interactions DOCK10 [1, 2]. Hfq protein monomers form a homohexameric ring that is thought to be the most active form of the protein [3, 4]. Much of what is known about

Hfq function is drawn from studies of loss of function alleles of hfq in bacteria including Escherichia coli[5], Salmonella typhimurium[6], and Vibrio cholerae[7]. A common hfq mutant phenotype is slow growth through exponential phase. However, loss of hfq function usually results in an array of mutant phenotypes, many of which are bacterium-specific. For example, E. coli hfq mutants exhibit slow growth in vitro[5], survive poorly in stationary phase, and are sensitive to both H2O2 and hyperosmotic conditions [8]. In contrast, hfq mutants in Vibrio cholerae grow reasonably well in vitro (though they exhibit impaired growth in a mouse infection model), survive normally in stationary phase, and are fully resistant to both H2O2 and hyperosmotic conditions [7]. Since many of the sRNAs that have been characterized require Hfq for their function, perhaps it is not surprising that loss of Hfq compromises a wide array of cellular processes.

Coll Surf B 2012, 92:209–212. 103. Klaus T, Joerger R, Olsson E, Granqvist CG: Silver-based crystalline nanoparticles, microbially fabricated. Proc Natl Acad Sci U S A 1999, 96:13611–13614. 104. Yong P, Rowson N, Farr JPG, Harris I, Macaskie L: Bioreduction and biocrystallization of palladium by Desulfovibrio EX 527 price desulfuricans NCIMB 8307. Biotechnol

Bioeng 2002, 80:369–379. 105. Corredor E, Testillano PS, Coronado MJ, González-Melendi P, Fernández-Pacheco R, Marquina C, Ibarra MR, de la Fuente JM, Rubiales D, Pérez-de-Luque A, Risueño MC: Nanoparticle penetration and transport in living pumpkin plants: in situ subcellular identification. BMC Plant Biol 2009, 9:45. 106. Taylor NJ, Fauquet CM: Microparticle bombardment as a tool in plant science and agricultural biotechnology. DNA Cell Biol 2002, 21:963–977. 107. BarathManiKanth S, Kalishwaralal K, Sriram M, Pandian SBRK, LCZ696 solubility dmso Youn H, Eom SH, Gurunathan S: Antioxidant effect of gold nanoparticles restrains hyperglycemic conditions in diabetic mice. J Nanobiotech 2010, 8:16. 108. Mohanpuria P, Rana NK, Yadav SK: Biosynthesis of nanoparticles: technological concepts and future applications. J Nanopart Res 2008, 10:507–517. 109. Wu H, Huang X, Gao M, Liao X,

Shi B: Polyphenol-grafted collagen fiber as reductant and stabilizer for one-step synthesis of size-controlled gold nanoparticles and their catalytic application to 4-nitrophenol reduction. Green Chem 2011, 13:651–658. 110. Ghosh S, Patil S, Ahire M, Kitture R, Gurav DD, Jabgunde AM, Kale S, Pardesi K, Shinde V, Bellare J, Dhavale DD, Chopade BA: Gnidia glauca flower extract mediated synthesis of gold nanoparticles and evaluation

of its chemocatalytic potential. J Nanobiotechno 2012, 10:17. 111. Vankar PS, Bajpai D: Preparation of gold nanoparticles from Mirabilis jalapa flowers. Ind J Biochem Biophys 2010, 47:157–160. 112. Das RK, Gogoi N, Bora U: Green synthesis ASK1 of gold nanoparticles using Nyctanthes arbortristis flower extract. Bioprocess Biosyst Eng 2011, 34:615–619. 113. Smitha SL, Philip D, Gopchandrana KG: Green synthesis of gold nanoparticles using Cinnamomum zeylanicum leaf broth. Spectro Acta A Mol Biomol Spectrosc 2009, 74:735–739. 114. Philip D: Rapid green synthesis of spherical gold nanoparticles using Mangifera indica leaf. Spectro Acta A Mol Biomol Spectrosc 2010, 77:807–810. 115. Noruzi M, Zare D, Khoshnevisan K, Davoodi D: Rapid green synthesis of gold nanoparticles using Rosa hybrida petal extract at room temperature. Spectro Acta A Mol Biomol Spectrosc 2011, 79:1461–1465. 116. Vanaja M, Paulkumar K, Baburaja M, Rajeshkumar S, Gnanajobitha G, Malarkodi C, Sivakavinesan M, Annadurai G: Degradation of methylene blue using biologically synthesized silver nanoparticles. Bioinor Chem App 2014, 742346:8. 117. Ganaie SU, Abbasi T, Anuradha J, Abbasi SA: Biomimetic synthesis of silver nanoparticles using the amphibious weed ipomoea and their application in pollution control.