ns: not significant, ** P < 0.01, *** P < 0.001. Discussion P. fluorescens is present at low level in the human gut and has been linked to Crohn's disease (CD) [7, 8], however little is known about the potential interaction of this bacterium with the intestinal mucosa. In the present paper, we aimed at determining its potential to adhere to IEC, to induce cell cytotoxicity and trigger a proinflammatory response. We selected two strains, a classical psychrotrophic strain (MF37) and a recently characterized clinical strain

adapted to grow at 37°C (MFN1032). The behaviour of these bacteria was compared to that of the opportunistic pathogen P. aeruginosa. Since adhesion and cytotoxicity to IECs are crucial events in the infection process, the three strains were tested on two epithelial cell lines. Except for adhesion, the two IECs models Selleck AZD1480 used in this study gave similar responses to the three strains of Pseudomonas. Indeed, a dose dependent adhesion of bacteria to Caco-2/TC7 and HT-29 cells was observed with the greatest effect obtained with the opportunistic pathogen P. aeruginosa. It is noteworthy that, compared to the psychrotrophic strain MF37, the clinical strain

P. fluorescens MFN1032, which is adapted to develop at 37°C displayed statistically significant higher adhesion potential to HT-29 but not selleck compound to Caco-2/TC7 cells. This observation suggests that the clinical strain may express a greater diversity of adhesion factors than MF37 and could explain, at least in part, the higher cytotoxicity effect of MFN1032. Although differences exist between surface proteins expressed by Caco-2/TC7 and HT-29 cell lines in comparison to normal human IECs, our results support the hypothesis that P. enough fluorescens should be able to colonize the intestinal

mucosa. ARN-509 chemical structure Pseudomonad are rarely searched for and detected as fecal bacteria, and are usually considered as a sub-dominant population [22]. In addition, there is now ample evidence that the circulating bacterial population in the intestinal lumen is very different from the resident microbiota that comes in contact with the apical surface of the enterocytes and is tightly associated to the mucus/glycocalyx layer [23, 24]. For an aerobic bacterium such as P. fluorescens, the best ecological niche should be at the vicinity of the epithelium, where oxygen concentration is the highest in the intestinal environment [25]. This is supported by the evidence showing that the P. fluorescens-specific I2 antigen sequence is systematically detected in ileal mucosa samples [7]. Moreover, in CD patients, there is a positive correlation between blood level of circulating anti-I2 antibodies and the severity of the disease [8] suggesting that the I2-producing bacteria, i.e. P. fluorescens, are in close contact with enterocytes and could contribute to CD pathogenesis. The LDH release assay showed that the cytotoxicity of P. fluorescens on Caco-2/TC7 and HT-29 cells is lower than that of P.

In the case of F. psychrophilum, P. ingrahamii and P. torquis, there were additional genes possessing sequences similar to the ssDNA binding domain. The product of the additional gene from F. psychrophilum was a protein of unknown function, while that from P. ingrahamii was the PriB. In P. torquis, it was a short (102 aa), single-stranded DNA binding protein without a characteristic sequence of last amino acid residues, in view of

which, we omitted that protein from our research. On the basis of the ssb gene organization and the number of ssb genes paralogs, bacteria have been classified in four different groups [21]. P. arcticus, P. cryohalolentis and P. profundum are classified as group III, which contains bacteria with ssb gene organization Dinaciclib ic50 uvrA-ssb, whereas D. psychrophila, F. psychrophilum, P. ingrahamii, and P. torquis are classified as group IV, which contains

bacteria with ssb placed neither between Danusertib datasheet rpsF and rpsR nor divergently located to uvrA. The DpsSSB, FpsSSB, ParSSB, PcrSSB, PinSSB, PprSSB, and PtoSSB proteins contain 142, 140, 213, 219, 222, 183, and 151 amino acid residues, respectively, including the N-terminal methionine, as is apparent from the nucleotide sequence. Analysis of the primary structures by RPS-BLAST revealed the presence of two distinctive regions in the proteins in question: one putative OB-fold domain, from amino acid 1 to 105–110, and one C-terminal domain, which contains four conserved terminal amino acid residues common in all known bacterial SSB proteins. The molecular mass of its monomers show a high differential, ranging from 15.6 to 25.1 kDa. Besides the OB-fold, the C-terminal fragment has the characteristic of a www.selleckchem.com/products/epacadostat-incb024360.html highly differential length, ranging from 31 to 112 amino acid residues. At their ends, the C-terminal domains have amino acids which are either similar or identical to the EcoSSB. The computable isoelectric point in these proteins has values in the

range of 5–6, which is typical for SSBs with Chloroambucil the exception of PinSSB, pI 7.79 (Table  1). Table 1 Characteristics resulting from the amino acid sequence analysis of the SSB proteins under study SSB Size of monomer [kDa] Length of sequence [aa] Length of C-terminal domain [aa] Sequence of last important amino acid residues pI Aliphatic index No. of Cys residues DpsSSB 15.6 142 37 DVPF 5.46 61.20 1 FpsSSB 15.9 140 31 DLPF 5.94 73.07 2 ParSSB 22.8 213 105 DIPF 5.91 49.11 0 PcrSSB 23.3 219 111 DIPF 5.70 43.29 0 PinSSB 25.1 222 112 DIPF 7.79 41.80 1 PtoSSB 17.1 151 43 DLPF 5.67 61.32 3 PprSSB 20.4 183 76 DIPF 5.43 54.37 0 EcoSSB 18.9 178 73 DIPF 5.44 56.97 0 Figure  1 shows the multiple amino acid alignment of the SSB proteins from the psychrophilic bacteria under study, from Shewanella woodyi (GenBank accession No. NC_010506; [22]), mesophilic E. coli (GenBank Accession No. NC_007779; [23]) and Bacillus subtilis (GenBank Accession No.

J Sci Ind Res 2009, 68:839–850. 4. Derylo-Marczewska AM, ABlachnio W, Marczewski B, Tarasiuk : Adsorption of selected herbicides from aqueous solutions on activated carbon. J Therm Anal Calorim 2010, 101:785–794.CrossRef 5. Modabber Ahmed K, Choong-Lyeal C, Dong-Hoon L, Man P, Bu-Kug GW2580 L, Jong-Yoon

L, Jyung-Choi : Synthesis and properties of mecoprop-intercalated layered double hydroxide. J Phys Chem Solids 2007, 68:1591–1597.CrossRef 6. Shukla G, Kumar A, Bhanti M, Joseph PE, Taneja A: Organochlorine pesticide contamination of ground water in the city of Hyderabad. Environ Int 2006, 32:244–247.CrossRef 7. Fernandez-Perez M, Gonzalez-Pradas E, Urene Amate MD, Wilkins RM, Lindrup I: Controlled release of imidacloprid from a lignin matrix: water release kinetics and soil mobility study. J Agric Food Chem 1998, 46:3828–3834.CrossRef 8. Otero R, Fernández JM, Ulibarri MA, Celis R, Bruna F: Adsorption of non-ionic pesticide S -metolachlor on layered double

hydroxides intercalated with dodecylsulfate and tetradecanedioate anions. Applied Clay Science 2012, 65:75–79. 9. Celis R, Hermosín MC, Cornejo J, Carrizosa MJ: Clay-herbicide complexes to retard picloram leaching in learn more soil. Int J Environ Anal Chem 2002, 82:503–517.CrossRef 10. Gerstl Z, Nasser A, Mingelgrin U: Controlled release of pesticides into soils from clay-polymer formulations. J Agric Food Chem 1998, 46:3797–3802.CrossRef 11. Hermosin MC, Calderon MJ, Aguer

JP, Cornejo J: MGCD0103 in vivo organoclays for controlled release of the herbicide fenuron. Pest Manag Sci 2001, 57:803–809.CrossRef 12. Unadabeytia T, Nir S, Rubin B: Organo-clay formulations of the hydrophobic herbicide norflurazon yield reduced leaching. J Agric Food Chem 2000, 48:4767–4773.CrossRef 13. Celis R, Koskinen WC, Hermosin MC, Ulibarri MA, Cornejo J: Triadimefon interactions with organoclays and organohydrotalcites. Soil Sci Soc Am J 2000, 64:36–43.CrossRef 14. Carrizosa MJ, Koskinen WC, Hermosin MC, Cornejo J: Organomestites as sorbent and carrier if the herbicide bentazone. Sci Total Environ 2000, 247:285–293.CrossRef 15. Carrizosa MJ, Koskinen WC, Hermosin MC, Cornejo J: Dicamba adsorption-desorption on organoclays. Appl Clay Sci 2001, 18:223–231.CrossRef 16. Lagaly G: Pesticide-clay interactions and formulations. Appl Clay Sci 2001, Molecular motor 8:265–275. 17. Nennemann A, Mishael Y, Nir S, Rubin B, Polubesova T, Bergaya F, Van Damme H, Lagaly G: Clay-based formulations of metolachlor with reduced leaching. Appl Clay Sci 2001, 18:265–275.CrossRef 18. Costantino U, Nocchetti M, Sisani M, Vivani R: Recent progress in the synthesis and application of organically modified hydrotalcites. Zeitschrift fur Kristallograhie 2009, 224:273–281. 19. Cavani F, Trifiro F, Vaccari A: Hydrotalcite-type anionic clays: preparation, properties and applications. Catal Today 1991, 11:173–301.CrossRef 20.

After the peptides Savolitinib ic50 common between hDM and hPNP were eliminated, 10 and 1 new possible binders that were generated as a result of Glu201Gln and Asn243Asp mutations respectively were identified. Although, hDM and C6 MH3B1 are both human derived proteins, novel MHCII binding peptides may result from their fusion. To address

this possibility, we also evaluated a 40 amino acid long peptide that included 14 amino acids from the C-terminus of hDM, the complete sequence of the α-helical linker and a 14 amino acids stretch of the N-terminus of C6 MH3B1 for possible MHCII binding peptides [16]. Only 6 potential MHCII binding peptides for all human MHCII alleles were identified VX-689 suggesting that minimal immunogenicity should result from the fusion of hDM to C6 MH3B1. Therefore, the probability of hDM-αH-C6 MH3B1 inducing a robust immune response in human should be minimal. Discussion In order to develop

a clinically relevant non-immunogenic therapeutic approach to ADEPT, we fused a mutant human enzyme to a human scFv specific for the HER2/neu tumor antigen. ADEPT requires both an active enzyme and the ability to AMN-107 target that enzyme to the tumor. Here we show that fusion of the mutant human PNP to the anti-HER2/neu scFv via an α-helical linker (hDM-αH-C6.5 MH3B1) results in an active protein that can be targeted to tumor cells, where it can cleave a relatively non-toxic mafosfamide prodrug to a cytotoxic drug, resulting in the inhibition of tumor cell proliferation. Previously it was shown that fusion of a 1.5 kDa short a nti- H ER2/n eu p eptide (AHNP) to the

C-terminus of hDM did not result in loss of enzyme activity [5]. We have now extended these studies to show that replacement of AHNP with the much larger (~50 kDa) scFv also did not significantly affect the activity of hDM (Table 1). In this fusion protein, a rigid α-helical linker was used to join the two domains. The spacing provided by the inflexible linker may minimize steric hinderace that could adversely influence the activity of either hDM or C6.5 MH3B1. Moreover, the C-terminus of the enzyme is extended away from the enzyme active site; therefore, fusion of a targeting component to the C-terminus of hDM should have a minimal affect on substrate binding and catalysis. Since hDM remains active after fusion to C6.5 MH3B1, it is reasonable to expect that following fusion of other scFvs with different specificities to hDM, the enzyme will remain active and capable of being targeted to other tumors. Therefore, the use of hDM is not restricted to HER/neu expressing tumors, but should be useful for ADEPT therapy of a wide variety of cancers. Fusion of hDM to the single chain C6.5 MH3B1 resulted in specific association of the enzyme activity with the HER2/neu expressing cells (Fig. 5A). C6.

aureus pathogenicity through their ability to bind fibronectin and fibrinogen and to initiate integrin-mediated intracellular uptake of the bacteria by non-professional phagocytes such as endothelial cells or osteoblasts [2, 3]. The invasion of host cells by S. aureus eventually leads to the formation of an intracytoplasmic

reservoir, where bacteria remain protected from the action of cell- and antibody-mediated immune response and from that of most antimicrobial agents. This bacterial sanctuarisation makes successful treatment even more challenging and paves the way for infection selleck compound relapse [4]. A peculiar difficulty to be faced in treating deep-seated infections is the risk of impaired diffusion of antimicrobial agents at the infection site, where they would BTK assay only achieve sub-inhibitory concentrations. S. aureus strains challenged with such antibiotic concentrations have been shown to exhibit altered phenotypes depending on the molecule tested, including down- or up-regulation of virulence factor expression. For example, beta-lactams enhance the secretion of virulence factors such as

the Panton-Valentine leukocidin and alpha haemolysin, while clindamycin or linezolid exert an inhibitory effect [5–8]. However, most studies on the antibiotic-mediated modulation

of protein expression by S. aureus have focused on secreted exotoxins, and less is known about this modulation with respect to MSCRAMMS, including FnBPA/B. In the present study, we aimed to investigate the impact of sub-inhibitory concentrations of major anti-staphylococcal agents on the adhesion and invasion phenotypes of S. aureus. After in vitro challenge of S. aureus 6-phosphogluconolactonase reference strain 8325-4 and clinical isolates with antibiotics, we SB202190 in vitro explored the following: (i) mRNA expression levels of the fnbA and fnbB genes, which encode FnBPA and B, respectively; (ii) bacterial adhesiveness to immobilised human fibronectin and human osteoblasts in culture; and (iii) bacterial invasion of human osteoblasts. Methods Bacterial strains The bacterial strains used in this study are summarised in Table 1. Laboratory strain 8325-4 and its ΔfnbA/B derivative DU5883 were used as a control for fnbA/B [9]. Clinical isolates were characterised for the presence of the fnbA, fnbB, agr1-4 and mecA genes by PCR as previously described [10, 11], and MLST was performed as described by Enright et al. to identify their genetic background [12].

FEBS Lett 2009, STA-9090 583:3425–3430.PubMedCrossRef 12. Steenhoudt O, Vanderleyden

J: Azospirillum , a free-living nitrogen fixing bacterium closely associated with grasses: genetic, biochemical and ecological aspects. FEMS Microbiol Lett 2000, 24:487–506.CrossRef 13. Kaur S, Mishra MN, Tripathi AK: Regulation of expression and biochemical characterization of a β-class carbonic anhydrase from the plant growth-promoting rhizobacterium, Azospirillum brasilense Sp7. FEMS Microbiol Lett 2009, 299:149–158.PubMedCrossRef 14. Aguilera J, van Dijken JP, de Winde JH, Pronk JT: Carbonic anhydrase (Nce103p): an essential biosynthetic enzyme for growth of Saccharomyces cerevisiae at atmospheric carbon dioxide pressure. Biochem J 2005, 391:311–316.PubMedCrossRef 15. Cunin R, Glansdorff N, Pierard A, Stalon V: Biosynthesis and metabolism of arginine in bacteria. Microbiol Rev 1986, 50:314–352.PubMed 16. Bergman NH, Passalacqua KD, Hanna PC, Qin ZS: Operon prediction for sequenced bacterial genomes without experimental information. Appl Environ Microbiol 2007, 73:846–854.PubMedCrossRef 17. Weerasinghe J, Dong T, Schertzberg M, Kirchhof M, Sun Y, Schellhorn H: Stationary phase expression of the arginine biosynthetic operon argCBH in Escherichia coli . BMC Microbiol 2006. Doi:10.1186/1471–2180–6-14 Epigenetics inhibitor 18. Parisi

G, Perales M, Fornasari M, Colaneri A, Schain N, Casati D, Zimmermann S, Brennicke A, Araya A, Ferry JG, Echave J, Zabaleta E: Gamma carbonic anhydrases in plant mitochondria. Plant Mol Biol 2004, 55:193–207.PubMedCrossRef 19. Merlin C, Masters M, McAteer S, Coulson A: Why is carbonic else anhydrase essential to Escherichia coli ? J Bacteriol 2003, 185:6415–6424.PubMedCrossRef 20. Mitra M, Lato SM, Ynalvez RA, Xiao Y, Moroney JV: Identification of a new chloroplast carbonic anhydrase in Chlamydomonas

reinhardtii . Plant Physiol 2004, 135:173–182.PubMedCrossRef 21. Fu X, Long-jiang Y, Mao-teng L, Wei L, Wu C, Yun-feng M: Evolution of structure in γ-class carbonic anhydrase and structurally related proteins. Mol Phylogenet Evol 2008, 47:211–220.PubMedCrossRef 22. Parisi G, Fornasari M, Echave J: Evolutionary analysis of γ-carbonic anhydrase and structurally related proteins. Mol Phylogenet Evol 2000, 14:323–334.PubMedCrossRef 23. Tatusov RL, Koonin EV, Lipman DJ: A genomic perspective on protein families. buy GF120918 Science 1997, 278:631–637.PubMedCrossRef 24. Vanstockem M, Michiels K, Vanderleyden J, Van Gool AP: Transposon mutagenesis of Azospirillum brasilense and Azospirillum lipoferum : physical analysis of Tn5 and Tn5- mob insertion mutants. Appl Environ Microbiol 1987, 53:410–415.PubMed 25. Karls RK, Wolf JR, Donohue TJ: Activation of the cyc A P2 promoter for the Rhodobacter sphaeroides cytochrome c 2 gene by the photosynthesis response regulator. Mol Microbiol 1999, 34:822–835.PubMedCrossRef 26.

Groups 1A and 2A showed significantly higher remissions compared with group 2B Fig. 8 Probability of cumulative CR (a) and CR + ICRI (b) for patients treated with PSL and CyA. Group A (1A + 2A) showed a significantly higher remission rate compared with group B (1B + 2B) in both analyses Four patients in group 1A were withdrawn from the study because of complications that may be related to CyA administration Cilengitide supplier (Table 3). In 3 of these 4 patients, C2 was >900 ng/mL, although there was no significant

difference in C2 between these 4 patients and the other 21 patients in group 1A. Discussion The combined administration of CyA with steroids has been reported to be useful for the treatment of IMN selleck with associated SRNS [5, 6, 18–20]. However, only a few randomized controlled trials have succeeded in clarifying this benefit [5, 6]. In the current randomized trial, we attempted to develop a more efficient strategy for CyA treatment by preprandial once-a-day administration. The effect of this method was significant for cumulative CR rate during 48 weeks using the Kaplan–Meier technique when compared with twice-a-day administration, but not for CR incidences at 48 weeks in the Fisher’s exact test. The discrepancy

of the results might be influenced by the relapsing cases because these were included in cumulative CR cases in the Kaplan–Meier technique. On the other hand, it was possible that scattered distribution of blood CyA concentrations in both groups might obscure the effect, although C2 in group 1 was significantly higher than group 2. ROC curve analysis was performed to assess the predictive value of blood CyA concentration for the outcome of NS. In comparison with C0, only C2 was available for predicting CR (Fig. 5). Interestingly, the predictive value of C2 was more enhanced when the hypercholesterolemic cases were excluded (Fig. 5). This study may demonstrate for the first time that hyperlipidemia in NS prevents CyA

treatment, although the affinity of CyA to lipoproteins has been studied in transplantation [21, 22]. The optimal cut-off points for C2 were calculated as 615 and 598 ng/mL of in all patients and in group 2, learn more respectively. As these results suggest that CyA might be effective for IMN when C2 is approximately >600 ng/mL, we divided each group into subgroups A (C2 ≥600 ng/mL) and B (C2 <600 ng/mL). Among these 4 subgroups, groups 1A and 2A showed significantly higher cumulative CR and CR + ICRI rates. Accordingly, regardless of whether the administration is once or twice a day, CyA blood concentration is a highly sensitive marker for the remission of NS. However, once-a-day administration seems to be more favorable because most of group 1 patients showed higher C2 concentrations.

After centrifugation cells were fixed in MeOH/acetic acid 3:1 overnight and then spread on slides. Hybridization with selleck kinase inhibitor rhodamine-coupled PNA was performed as described [23]. For each sample 20 metaphases per slice on triplicate were scored. Images of the metaphases were captured with a 100 × objective. Chromatin immunoprecipitaion assay (ChIP) BJ-EHLT fibroblasts

were treated for 24 hrs with 0.5 μM of the compound. ChIP selleck assay was performed as previously described [24]. The following antibodies were used: pAb anti-TRF1 (Santa Cruz Biotechnology, Santa Cruz, Ca); mAb anti-TRF2 (Imgenex, San Diego, CA); pAb anti-POT1 (Abcam). mAb anti-β-actin (Sigma) was used as negative control of the ChIP assay. Results and discussion Synthesis of quino [4,3,2-kl] acridinium salts We have previously reported two routes to the pentacyclic acridinium salt 1. The less efficient involved construction of the 1-bromo-7-fluoro-3-methylacridone 4 selleck products which was processed to the intermediate N-methylacridone 5 where the pivaloyl-protected fluoroaniline fragment was attached by a Suzuki coupling.18 Deprotection and cyclization of 5 in EtOH–5 M HCl yielded the pentacycle 6 in 65% yield (Figure 

2). Methylation of 5 with dimethyl sulphate in refluxing nitromethane furnished the dark red pentacyclic salt 1 (48%). However the overall yield of 1 from suitable precursors to 4 was disappointingly low at < 10% [20]. A more practicable route for the large-scale synthesis of salt 1 involved the multi-step, but ‘one-pot’, conversion of the N-methylquinolinium methosulfate salt 7 to 1 with triethylamine in nitrobenzene at 120°C in an optimized 33% yield [21]. This surprising process was adapted from a synthesis of salts related to 1 by Ozczapowicz and

colleagues in 1988 [21]. Figure 2 (I) NaH in DMF, Me 2 SO 4 ; (II) 5-fluoro-2-pivalamidophenylboronic acid, Pd(PPh 3 ) 4 , NaHCO 3 , aq. DME, 80°C; (III) EtOH, 5 M HCl; (IV) Me 2 SO 4 in MeNO 2 , reflux; (V) Et 3 N in nitrobenzene, 120°C, 24 h; (VI) EtOSO 2 CF 3 , CHCl 3 , 140°C, 72 h. Efforts to prepare higher alkyl homologues of 1 were Tolmetin only partially successful presumably because access by larger alkylating moieties at N-13 of pentacycle 6 were impeded by hydrogen atoms at positions 1 and 12 (for numbering system see Figure  1): thus whereas the N-ethyl quaternary salt 8 (20%) could be prepared with difficulty by heating 6 and ethyl trifluoromethane sulfonate in chloroform under nitrogen at 140°C in a sealed tube for 3 days, it was not possible to prepare n-propyl or i-propyl homologues of 6 under a range of forcing conditions. The isomeric N-acetyl compounds 2 and 3 were prepared starting from the 2-aminoquinoacridine 9 or 3-chloroquinoacridine 10, respectively, in several steps according to our previously published work [25].

It is worth to note that dielectric-capped isolated metal nanospheres have already demonstrated their effective applicability in photovoltaics [15] and SERS [16]. Here we present our studies on the influence of a high-index TiO2 ALD spacer on the SPR position and

SERS intensity in the case of silver island films grown on soda-lime glass substrates using our recently developed silver out-diffusion (SOD) technique [17]. It is important to note that MIFs are highly fragile and, therefore, they must be protected for any practical use. The use of conformally grown ALD films is ideal for protecting MIFs with a cover layer, since the layer thickness can be controlled at an atomic level and the initial 4SC-202 surface relief structure can be maintained with thin cover layer thicknesses [18]. In the experiments, we varied the thickness of the ALD TiO2 spacer and HDAC inhibitor the MIF structure. The interest in TiO2 spacers is twofold: (1) the high catalytic abilities

of TiO2 [19–21] allowing the use of SERS with a titanium dioxide spacer in nanoscale organic and biochemistry studies and (2) the high refractive index of TiO2 providing stronger control of the ALD-coated MIF structure, which results in wider spectral tunability of the system. Methods MIF formation and characterization GANT61 molecular weight We fabricated silver nanoisland films using SOD from glass in the course of the ion-exchanged glass substrate annealing in a reducing hydrogen atmosphere. In the experiments, we used soda-lime glass microscope slides produced Tacrolimus (FK506) by Menzel [22]. The silver-sodium ion exchange was performed at 325°C in an ion-exchange bath containing 5 wt.% of silver nitrate and 95 wt.% of sodium nitrate as was reported elsewhere [23]. One-millimeter-thick slides

with a size of 20 × 30 mm2 were immersed in the melt for 20 min, which provided a few microns of silver penetration depth in the glass. Optical absorption spectroscopy of the ion-exchanged slides did not show any absorption peaks in the spectral range corresponding to the surface plasmon resonance, which indicated the absence of silver nanoparticles both in the bulk and on the surface of the slides. The ion-exchanged slides were annealed in hydrogen for 10 min to reduce silver ions to atoms and get a supersaturated solid solution of neutral silver in the glass matrix. According to the proposed mechanism [24], this results in the formation of both silver nanoparticles within the glass and a silver island film on the glass surface (MIF) due to the out-diffusion of silver atoms. After the MIF formation, we measured the optical absorption spectra of the samples using a Specord 50 spectrophotometer (Analytik Jena AG, Jena, Germany).

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MM, Santini L, Medaglini D, Pozzi G: Intranasal immunization of mice with recombinant Streptococcus gordonii expressing NadA of Neisseria meningitidis induces systemic bactericidal antibodies and local IgA. Vaccine 2008,26(33):4244–4250.PubMedCrossRef 23. Bowe F, Lavelle EC, McNeela EA, Hale C, Clare S, Arico B, Giuliani MM, Rae A, Huett A, Rappuoli R, Dougan G, Mills KH: Mucosal vaccination against serogroup B meningococci: induction of bactericidal antibodies and cellular immunity following intranasal immunization with NadA of Neisseria meningitidis and mutants

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