mallei and B. pseudomallei [2, 9, 16–18, 22, 41, 43–49]. Several gene products, such as BimA, type 3 secretion system effectors, and type 6 secretion proteins, have been shown to play key roles in this process. By contrast, the mechanisms used by these organisms to adhere to eukaryotic cells are poorly defined. Adherence is an essential step of pathogenesis by most infectious agents because it is necessary for colonizing a new host [50–52]. Moreover, B. pseudomallei and B. www.selleckchem.com/products/jq1.html mallei are facultative intracellular pathogens that gain access to the interior

of target cells. Though not always a prerequisite for this process, bacterial adherence is a widespread strategy that precedes and promotes invasion [50–52]. Thus far, only the B. pseudomallei flagellum [53] and type 4 pilus [54] have been implicated in adherence and their exact roles remain to be elucidated. The present study reports the identification of B. pseudomallei and B. mallei gene products that mediate adherence to epithelial cells derived from the NVP-AUY922 human respiratory tract, thus relevant to the aerosol route of infection by these organisms. Results Identification of a gene shared by B. mallei and B. pseudomallei that

encodes a potential autotransporter adhesin Analysis of the annotated genomic sequence of B. mallei ATCC23344 identified the ORF locus tag number BMAA0649 as resembling members of the oligomeric coiled-coil adhesin (Oca) family of autotransporter proteins [55]. Yersinia enterocolitica YadA [55–57] is the prototypical member of this group of adherence factors, which also includes Haemophilus influenzae Hia [58–60] and HA-1077 clinical trial Moraxella catarrhalis Hag [61, 62]. These Oca proteins share structural

features including a C-terminal outer membrane (OM) anchor domain composed of 4 β-strands (also referred to as the transporter module), a surface-exposed passenger domain often containing repeated amino acid (aa) motifs, and a helical region of ~40 residues that connects the OM anchor to the surface-exposed passenger domain [55, 63–65]. As illustrated in Fig 1A, BMAA0649 is predicted to possess these features. Further sequence analysis of the B. mallei ATCC23344 gene product revealed that residues 208-362 (and 1010-1149) contain repeats with the consensus xxxAVAIGxx[N/A]xAx (open circles in Fig 1A), which resemble motifs found in the N-terminus of Y. enterocolitica YadA (xxxSVAIGxxSxAx) [56, 57] and M. catarrhalis Hag (GxxSIAIGxx[A/S]xAx) [61]. In YadA, these AIG patterns have been shown to form a structure termed a β-roll and to specify adhesive properties. The passenger domain of BMAA0649 was also found to contain several serine-rich repeats beginning with residues SLST (colored squares in Fig 1A). Additionally, searches using the Pfam database indicated that aa 1456-1535 of BMAA0649 encode a YadA-like C-terminal domain (PF03895; expect value 3.

For time contrast 6–3 weeks, one gene was up-regulated (log FC 1.0). DLEC1, Deleted in lung and esophageal cancer 1, a tumor suppressor gene that may be a potential

negative regulator of cell proliferation [29]. Top table analysis resection group All discussed genes in this chapter are illustrated in Figure 4. Amongst up-regulated genes in the resection group there was in early time period (from t = 0 until t = 1), a predominance of genes regulating transcription, intracellular and cell-cell signalling, extracellular matrix/cytoskeleton and inflammation, whereas genes governing the cell cycle were evenly expressed throughout the experiment. Towards the end of the experiment (from t = 1 until t = 2), we found an increase in up-regulation for genes controlling lipid, hormone, amine, alcohol metabolism and transport. Figure 4 Functional classification of all C646 manufacturer genes according to Online Mendelian Inheritance in Man and Ace View. Amongst down-regulated genes in the resection group there was an increase in

number of genes controlling cell cycle and transcription towards the end of the experiment (from t = 1 until t = 2). Genes regulating transport, inflammation and lipid, hormone, amine, alcohol metabolism and transport were only down-regulated in the earliest time period (from t = 0 until t = 1). Paclitaxel nmr The expressions of genes regulating cell proliferation were down-regulated at three weeks, whereas genes regulating protein metabolism remained stable. We found a predominance of down-regulated genes regulating intracellular and cell-cell signalling towards the end of liver regeneration. Top table analysis sham group Amongst up-regulated genes within the sham group, we found from t = 0 until t = 2 a gradual increase in the differential expression of genes controlling cell cycle, transcription and transport. From t = 1 until t = 2, there was a gradual increase in the differential expression of genes governing translation.

From t = 0 until t = 1 there was a gradual decrease in expression of genes regulating protein metabolism. In addition, genes regulating intracellular and cell-cell signalling decreased towards the end of the experiment. Genes regulating BCKDHA inflammation and extracellular matrix/cytoskeleton were only up-regulated from t = 0 until t = 1. Amongst down-regulated genes in the sham group, there was a decrease in down-regulation of genes controlling cell cycle, transcription, transport, extracellular matrix/cytoskeleton and lipid, hormone, amine, alcohol metabolism from t = 0 until t = 1. However, genes controlling transcription, transport, protein metabolism and lipid, hormone, amine, alcohol metabolism increased again towards the end of the experiment. Down-regulated genes controlling intracellular and cell-cell signalling increased in expression from t = 0 until t = 2, whereas genes regulating cell proliferation decreased over all time periods.

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P < 0.05 was considered to www.selleckchem.com/products/icg-001.html be significant in all cases. Acknowledgements This work was carried out through a PhD Programme in Molecular Cell Biology funded by the Programme for Research in Third-Level Institutions (PRTLI) awarded to AC. Work in the authors’ laboratory is supported by the Irish Government under the National Development Plan; by the Irish

Research Council for Science Engineering and Technology (IRCSET); by Enterprise Ireland; and by Science Foundation Ireland (SFI), through the Alimentary Pharmabiotic Centre (APC) at University College Cork, Ireland, which is supported by the SFI-funded Centre for Science, Engineering and Technology (SFI-CSET) and provided PDC, CH and RPR with SFI Principal Investigator funding. References 1. Rogers LA, Whittier EO: Limiting factors in the lactic fermentation. J Bacteriol 1928, 16:211–229.PubMed 2. Chen H, Hoover DG: Bacteriocins and their food applications. Comprehensive Rev Food Sci Food Safety 2003, 2:82–100. 3. Delves-Broughton J: Nisin and

its uses as a food preservative. Food Technol 1990, 44:100–117. 4. Guinane CM, Cotter PD, Hill C, Ross RP: Microbial solutions to microbial problems; lactococcal bacteriocins for the control of undesirable selleck kinase inhibitor biota in food. J Appl Microbiol 2005, 98:1316–1325.PubMedCrossRef 5. de Vos WM, Kuipers OP, van der Meer JR, Siezen RJ: Maturation pathway of nisin and other lantibiotics: post-translationally modified antimicrobial peptides exported by Gram-positive bacteria. Mol Microbiol 1995, 17:427–437.PubMedCrossRef 6. Sahl H, Jack R, Bierbaum G: Biosynthesis and biological activities of lantibiotics with unique post-translational modifications. Eur J Biochem 1995, 230:827–853.PubMedCrossRef buy Metformin 7. Bierbaum G, Sahl HG: Lantibiotics: mode of action, biosynthesis and bioengineering. Curr Pharm Biotechnol 2009, 10:2–18.PubMedCrossRef 8. Hsu ST, Breukink E, Tischenko E, Lutters MA, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA: The nisin-lipid II complex reveals a pyrophosphate cage that

provides a blueprint for novel antibiotics. Nat Struct Mol Biol 2004, 11:963–967.PubMedCrossRef 9. Wiedemann I, Breukink E, van Kraaij C, Kuipers OP, Bierbaum G, de Kruijff B, Sahl HG: Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. J Biol Chem 2001, 276:1772–1779.PubMed 10. Wiedemann I, Benz R, Sahl HG: Lipid II-mediated pore formation by the peptide antibiotic nisin: a black lipid membrane study. J Bacteriol 2004, 186:3259–3261.PubMedCrossRef 11. Cotter PD, Hill C, Ross RP: Bacterial lantibiotics: strategies to improve therapeutic potential. Curr Protein Pept Sci 2005, 6:61–75.PubMedCrossRef 12. Piper C, Cotter PD, Ross RP, Hill C: Discovery of medically significant lantibiotics. Curr Drug Discov Technol 2009, 6:1–18.PubMedCrossRef 13.

coli strains upon changes in growth temperature [13]. Expression of FabF1 restored cis-vaccenate synthesis at all temperatures,

but was much more effective at 30°C than at 37°C or 42°C (Table 1). This effect seems likely to be due to the effects of temperature on FabF1 synthase activity since thermal regulation disappeared upon X-396 manufacturer expression of FabF1 from a high copy number vector (Table 1) and the enzyme was thermolabile in vitro (see below). Apparently, at high growth temperatures low levels FabF1 elongation activity was overcome by high-level expression of the protein. We also found high levels of cis-vaccenate at the non-permissive temperature upon expression of fabF1 in an E. coli fabB fabF strain that carried the fabB gene of Haemophilus influenzae, INCB024360 cost a bacterium naturally defective in both cis-vaccenate synthesis and in regulation of fatty acid composition by temperature [14] (data not shown).

Table 1 Effects of growth temperature on fatty acid compositions (% by weight)of fabF strain MR52 carrying plasmids encoding C. acetobutylicium fabF1.   30°C 37°C 42°C Fatty acid pHW33 pHW36 pHW33 pHW36 pHW33 pHW36 C14:0 2.2 5.8 2.4 6.2 2.6 3.3 C16:1 40.3 29 35 24.8 53.4 28.9 C16:0 21.4 25.8 32.4 25.1 26.2 28.7 C18:1 33.3 30 25.9 32.4 14.8 30.2 C18:0 2.8 9.4 4.3 11.6 2.9 8.7 Figure 2 Growth of E. coli strains CY242, K1060, CY244, and JWC275 transformed with plasmids encoding the C. acetobutylicium fabF homologues. Following induction by addition of arabinose, transformants of strain K1060 were grown at 37°C, whereas the transformants of strains CY242, strain CY244 and strain JWC275 were grown at 42°C. The strains carried plasmids pHW36, pHW37 or pHW38 encoding fabF1, fabF2 and fabF3, respectively, or the vector plasmid, pBAD24. The C. acetobutylicium fabF1 gene can functionally replace

E. coli FabB Although the presence of plasmid pHW36 (fabF1) PJ34 HCl allowed growth of the two E. coli fabB(Ts) fabF strains at the non-permissive temperature, growth of both strains required oleate. The lack of growth in the absence of oleate argued that either FabF1 lacked the ability to replace FabB or that FabF1 was unable to simultaneously perform the tasks of both FabB and FabF under these conditions. To decide between these alternatives we transformed pHW36 into strain K1060, a strain that carries an unconditional fabB allele, and into strain CY242 which carries the same fabB(Ts) allele as strain CY244. The complementation experiments showed that C. acetobutylicium fabF1 allowed strain K1060 to grow on RB medium lacking oleate at 37°C (Fig. 2). However, fabF1 failed to complement growth of the temperature sensitive fabB mutant strain, CY242 at 42°C (Fig. 2). If FabF1 possessed FabB activity at 37°C, unsaturated fatty acids should be synthesized.

Three independent experiments done in triplicate were realized. Statistical analysis Data are

expressed as mean +/- standard deviation (SD). Statistical analysis was performed with Student’s t test. A p value < 0.05 was considered statistically different. Nucleotide sequence accession number The DNA sequence reported in this paper has been deposited in GenBank under accession number JF699754. Acknowledgements This study was supported by the Institut National de la Recherche Agronomique (INRA) and the Ministère de l'Education Nationale de la Recherche et de la Technologie (MENRT). We thank N. Rouhier for his technical advices and his technical supports. We thank S. Payot-Lacroix and M. Genay-Bernard for critical reading of the manuscript. References 1. Kosikoski FV, Mistry VV: Volume 1: Origins and Principles. 1997. in Cheese Selleckchem A769662 and Fermented Milk Foods, r.e. Westport, Editor. 2. Wouters JA, Rombouts FM, de Vos WM, Kuipers OP, Abee T: Cold shock proteins and low-temperature response of Streptococcus thermophilus CNRZ302. Appl Environ Microbiol 1999,65(10):4436–42.PubMed 3. Perrin C, Guimont C, Bracquart P, Gaillard

JL: Expression of a new cold shock protein of 21.5 kDa and of the major cold shock protein by Streptococcus thermophilus after cold shock. Curr Microbiol 1999,39(6):342–0347.PubMedCrossRef 4. Varcamonti M, Arsenijevic S, Martirani L, Fusco D, Naclerio G, De Felice M: Expression of the heat shock gene clpL Roscovitine in vitro of Streptococcus thermophilus is induced by both heat and cold shock. Microb Cell Fact 2006, 5:6.PubMedCrossRef 5. Martirani L, Raniello R, Naclerio G, Ricca E, De Felice M: Identification of the DNA-binding protein, HrcA, of Streptococcus thermophilus. FEMS Microbiol Lett 2001,198(2):177–82.PubMedCrossRef 6. Derre I, Rapoport G, Msadek T: CtsR, a novel regulator of stress and heat shock response,

controls clp and molecular Orotidine 5′-phosphate decarboxylase chaperone gene expression in gram-positive bacteria. Mol Microbiol 1999,31(1):117–31.PubMedCrossRef 7. Kilstrup M, Jacobsen S, Hammer K, Vogensen FK: Induction of heat shock proteins DnaK, GroEL, and GroES by salt stress in Lactococcus lactis . Appl Environ Microbiol 1997,63(5):1826–37.PubMed 8. Zotta T, Asterinou K, Rossano R, Ricciardi A, Varcamonti M, Parente E: Effect of inactivation of stress response regulators on the growth and survival of Streptococcus thermophilus Sfi39. Int J Food Microbiol 2009,129(3):211–20.PubMedCrossRef 9. Fleuchot B, Gitton C, Guillot A, Vidic J, Nicolas P, Besset C, Fontaine L, Hols P, Leblond-Bourget N, Monnet V, Gardan R: Rgg proteins associated with internalized small hydrophobic peptides: a new quorum-sensing mechanism in streptococci . Mol Microbiol 2011,80(4):1102–19.PubMedCrossRef 10. Neely MN, Lyon WR, Runft DL, Caparon M: Role of RopB in growth phase expression of the SpeB cysteine protease of Streptococcus pyogenes . J Bacteriol 2003,185(17):5166–74.PubMedCrossRef 11.

Mol Plant Microbe Interact 2011,24(6):631–639.PubMedCrossRef this website 3. Tian CF, Garnerone AM, Mathieu-Demazière C, Masson-Boivin C, Batut J: Plant-activated bacterial receptor adenylate cyclases modulate epidermal infection in the Sinorhizobium meliloti-Medicago symbiosis. Proc Natl Acad Sci USA 2012,109(17):6751–6756.PubMedCentralPubMedCrossRef 4. He Y, Li N, Chen Y, Chen X, Bai J, Wu J, Xie J, Ying H: Cloning, expression, and characterization

of an adenylate cyclase from Arthrobacter sp. CGMCC 3584. Appl Microbiol Biotechnol 2012,96(4):963–970.PubMedCrossRef 5. McDonough KA, Rodriguez A: The myriad roles of cyclic AMP in microbial pathogens: from signal to sword. Nat Rev Microbiol 2012,10(1):27–38. 6. PD-332991 Linder JU: Class III adenylyl cyclases: molecular

mechanisms of catalysis and regulation. Cell Mol Life Sci 2006,63(15):1736–1751.PubMedCrossRef 7. Masson-Boivin C, Giraud E, Perret X, Batut J: Establishing nitrogen-fixing symbiosis with legumes: how many rhizobium recipes? Trends Microbiol 2009,17(10):458–466.PubMedCrossRef 8. Shenroy AR, Visweswariah SS: Class III nucleotide cyclases in bacteria and archaebacteria: lineage-specific expansion of adenylyl cyclases and a dearth of guanylyl cyclases. FEBS Lett 2004,561(1–3):11–21.PubMedCrossRef 9. Kimura Y, Mishima Y, Nakano H, Takegawa K: An adenylyl cyclase, CyaA, of Myxococcus xanthus functions in signal transduction during osmotic stress. J Bacteriol 2002,184(13):3578–3585.PubMedCentralPubMedCrossRef 10. Kimura Y, Ohtani M, Takegawa K: An adenylyl cyclase, CyaB, acts as an osmosensor in Myxococcus xanthus. J Bacteriol 2005,187(10):3593–3598.PubMedCentralPubMedCrossRef 11. Agarwal N, Lamichhane G, Gupta R, Nolan S, Bishai WR: Cyclic AMP intoxication of macrophages by a Mycobacterium tuberculosis adenylate cyclase. Nature 2009,460(7251):98–102.PubMedCrossRef 12. Agarwal N, Bishai WR: cAMP signaling in Mycobacterium tuberculosis. Indian J Exp Biol 2009,47(6):393–400.PubMed 13. Topal H, Fulcher NB, Bitterman J, Salazar E, Buck J, Levin

LR, Cann MJ, Wolfgang Rucaparib cell line MC, Steegborn C: Crystal structure and regulation mechanisms of the CyaB adenylyl cyclase from the human pathogen Pseudomonas aeruginosa. J Mol Biol 2012,416(2):271–286.PubMedCentralPubMedCrossRef 14. Hall RA, De Sordi L, Maccallum DM, Topal H, Eaton R, Bloor JW, Robinson GK, Levin LR, Buck J, Wang Y, et al.: CO(2) acts as a signalling molecule in populations of the fungal pathogen Candida albicans. PLoS Pathog 2010,6(11):e1001193.PubMedCentralPubMedCrossRef 15. Xu XL, Lee RT, Fang HM, Wang YM, Li R, Zou H, Zhu Y, Wang Y: Bacterial peptidoglycan triggers Candida albicans hyphal growth by directly activating the adenylyl cyclase Cyr1p. Cell Host Microbe 2008,4(1):28–39.PubMedCrossRef 16. Capela D, Barloy-Hubler F, Gouzy J, Bothe G, Ampe F, Batut J, Boistard P, Becker A, Boutry M, Cadieu E, et al.: Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021.

Reduction 3: to \(N_x,N_y,\varrho_x,\varrho_y\) In this case our aim is to retain only information on the number and typical size of crystal distribution, so we eliminate the dimer concentrations x, y, using $$ \lambda_x = \frac\varrho_x2 N_x , \quad \lambda_y = \frac\varrho_y2 N_y , \quad x = \frac2 N_x^2\varrho_x ,

\quad y = \frac2 N_y^2\varrho_y . $$ (5.46)These transformations reformulate the governing Eqs. 5.1–5.6 to $$ \frac\rm d N_x\rm d t = \frac12 \mu (\varrho -R) + \beta N_x – 2 (\mu\nu+\beta) \fracN_x^2\varrho_x – \frac2\xi N_x^3\varrho_x ,\\ $$ (5.47) $$ \frac\rm d N_y\rm d t = \frac12 \mu (\varrho – R) + \beta N_y – 2 (\mu\nu+\beta) \fracN_y^2\varrho_y – \frac2\xi N_y^3\varrho_y , \\ $$ (5.48) $$ \frac\rm d \varrho_x\rm d t = (\varrho-R)(\mu+\alpha N_x) – \frac4\mu\nu

N_x^2\varrho_x Sorafenib datasheet , \\ $$ (5.49) $$ \frac\rm d \varrho_y\rm d t = (\varrho-R)(\mu+\alpha N_y) – \frac4\mu\nu N_y^2\varrho_y , $$ (5.50)where \(R := \varrho_x + buy Temozolomide \varrho_y\). We now transform to total concentrations (N, R) and relative chiralities (ϕ and ζ) via $$ N_x = \frac12 N (1+\phi) , \quad N_y = \frac12 N (1-\phi) , \quad \varrho_x = \frac12 R (1+\zeta) , \quad \varrho_y = \frac12 R (1-\zeta) , $$ (5.51)together with \(c = \frac12 (\varrho – R)\), to obtain $$ \frac\rm d R\rm d t = (\varrho-R)(2\mu+ \alpha N) – \frac4\mu\nu N^2(1+\phi^2-2\phi\zeta)R (1-\zeta^2) , \\ $$

(5.52) $$ \beginarrayrll \frac\rm d N\rm d t & = & \mu (\varrho – R) + \beta N \\ && – \fracN^2R(1-\zeta^2) \left[ 2(\mu\nu+\beta) (1+\phi^2-2\phi\zeta) + \xi N (1+3\phi^2-3\phi\zeta-\phi^3\zeta) \right] , \\ \endarray $$ (5.53) $$ \beginarrayrll \frac\rm d\phi\rm d t &=& \beta\phi – \frac1N\frac\rm d N\rm d t\phi \\&& – \fracNR(1-\zeta^2) \left[ 2(\beta+\mu\nu)(2\phi-\zeta-\phi^2\zeta) + \xi N (3\phi-\zeta+\phi^3-3\phi^2\zeta) \right] , \\ \endarray $$ (5.54) $$ \frac, \zeta\rm d t = \frac\alpha (\varrho-R) N \phiR – \frac1R\frac\rm d R\rm d t \zeta – \frac4\mu\nu N^2 (2\phi-\zeta-\phi^2\zeta)R^2 (1-\zeta^2) . $$ (5.55)We now analyse this system in more detail, since this set of equations conserves mass, and is easier to analyse than Eqs. 5.33–5.35 due to the absence of square roots. We consider the two asymptotic limits (β ≪ 1 and α ∼ ξ ≫ 1) in which, at steady-state, the majority of mass is in the form of clusters. The Symmetric Steady-State Putting ζ = 0 = ϕ, we find the symmetric steady-state is given by $$ 0 = (\varrho-R)(2\mu+\alpha N) – \frac4\mu\nu N^2R , \\ $$ (5.56) $$ 0 =f \mu (\varrho-R) + \beta N – 2(\mu\nu+\beta)\fracN^2R – \frac\xi N^3R . $$ (5.

The in vitro effects on NF-κB augmentation has been reported to be dependent on lactobacilli viability, since after heat-killing they only had a marginal effect on NF-κB activation in co-stimulation experiments with E. coli. This supports modulation of NF-κB as a potential probiotic mechanism. The ability of probiotic lactobacilli to interfere with UPEC colonization in the vagina, and thereby the pathogens’ ascension into the bladder, could therefore involve immunomodulatory activity,

specifically via NF-κB activation. Conclusions The main cause of UTI is ascending E. coli that colonizes the vagina, urethra then bladder. To remove unwanted pathogens, the urothelial cells of the mucosa carry Galunisertib molecular weight specific receptors, such as TLR4 that can recognize the most common Gram-negative species. Once these receptors bind the cognate bacterial ligand, the epithelial cells respond by producing a range of compounds including cytokines that are strongly regulated by the NF-κB transcription factor. The present in vitro study showed that this immune activation could be amplified by probiotic L. rhamnosus GR-1. Moreover, augmentation of NF-κB was accompanied by an increase in inflammatory TNF expression. The important recognition molecule TLR4 was found to be up-regulated by L. rhamnosus GR-1 on both mRNA and protein level in cells concomitantly challenged with E. coli.

Moreover, the blocking agonist binding to TLR4 completely inhibited the augmentation of NF-κB by L. rhamnosus GR-1. Due to the importance IKBKE of TLR4 in the process of pathogen clearance we suggest that this represents selleck a pathway in which probiotic immunomodulatory lactobacilli work to increase immunity and prevent infections. Methods Cell culture The T24 human bladder carcinoma cell line (ATCC HTB-4) was cultured in RPMI 1640 (Hyclone) supplemented with 2.05 mM of L-glutamine and 10%

fetal bovine serum (FBS; Hyclone) at 37°C with 5% CO2 in a humidified environment. Bacterial strains and growth conditions L. rhamnosus GR-1 (urethral isolate) and GG (intestinal isolate) were cultured on de Man Rogosa Sharp (MRS) agar (Difco) anaerobically using anaerobic packs (BD) at 37°C for 24 h under static condition. For cell culture challenge, lactobacilli were grown from a 1% inoculum in MRS broth for 24 h followed by washing and resuspending in the original volume with phosphate buffered saline (PBS; pH 7.4). Uropathogenic E. coli GR12 was grown in Luria-Bertani (LB) medium (Difco) at 37°C and constant shaking. Heat-killed bacteria were prepared by washing cultures in PBS and heating at 70°C for 1 h followed by plating 100 μl on the respective growth medium (MRS or LB) to confirm loss of viability. Heat-killed L. rhamnosus GR-1 and E. coli were stored at -20°C until used for cell challenge.

(2) The refractive index sensitivity of single-mode LSPR in nanoparticles is independent of the resonance mode of choice and the particle geometry provided that the sensing wavelength is fixed. (3) The improved FOM observed for plasmonic quadrupole resonances in gold nanoparticles in the present work as well as in previous R788 solubility dmso studies is due mainly to the reduction of resonance

linewidth. Our results suggest that plasmonic quadrupole modes in gold nanorods are possibly the most promising choice to achieve the best sensing performance and that it is of particular importance to explore multipolar resonances for further sensing studies. Acknowledgements This work was supported by the Hong Kong Polytechnic University (Projects 1-ZVAL, 1-ZVAW, and A-PL53), and the National High Technology Research and Development Program of China (863 Program) under Grant 2013AA031903. The authors

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