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complex CP24 affects the structure and function of the grana membranes of higher plant chloroplasts. Plant Cell 18:3106–3120. doi:10.​1105/​tpc.​106.​045641 PubMedCrossRef Lambrev PH, Várkonyi much Z, Krumova S, Kovács L, Miloslavina Y, Holzwarth AR, Garab G (2007) Importance of trimer-trimer interactions for the native state of the plant light-harvesting complex II. Biochim Biophys Acta Bioenerg 1764:847–853CrossRef Lepetit B, Volke D, Szabó M, Hoffmann R, Garab G, Wilhelm C, Goss R (2007) Spectroscopic and molecular characterization of the oligomeric antenna of the diatom Phaeodactylum tricornutum. Biochemistry 46:9813–9822. doi:10.​1021/​bi7008344 PubMedCrossRef Liu ZF, Yan HC, Wang KB, Kuang TY, Zhang JP, Gui LL, An XM, Chang WR (2004) Crystal structure of spinach major light-harvesting complex at 2.72 angstrom resolution. Nature 428:287–292. doi:10.​1038/​nature02373 PubMedCrossRef Louwe RJW, Vrieze J, Hoff AJ, Aartsma TJ (1997) Toward an integral interpretation of the optical steady-state spectra of the FMO-complex of Prostecochloris aestuarii. 2 Exciton simulation. J Phys Chem B 101:11280–11287. doi:10.​1021/​jp9722162 CrossRef Morosinotto T, Breton J, Bassi R, Croce R (2003) The nature of a chlorophyll ligand in Lhca proteins determines the far red fluorescence emission typical of photosystem I. J Biol Chem 278:49223–49229. doi:10.​1074/​jbc.

5 mL microfuge tube, air dried briefly and suspended in 200 μL TE buffer resulting in a DNA concentration of approximately 1 μg/μL. Sequencing and annotation Random and φ52237-sequence guided φX216 genome fragment clones were constructed by this website restriction digest of purified φX216 genomic DNA with EcoRI, EcoRI + HindIII or AgeI and ligation with EcoRI, EcoRI + HindIII or SmaI digested pUC19 DNA [25], respectively, followed by

transformation of E. coli DH5α or GBE180 [26] using standard transformation protocols [27] and recovery of white colonies on LB plates containing 100 μg/mL ampicillin and 50 μg/mL 5’-bromo-4-chloro-3-indolyl-β-D-galactopyranoside (X-gal). φ52237-sequence-guided PCR amplicons were designed to close gaps and confirm fragment clone borders. Sequencing was accomplished using M13F and M13R primers, as well as φ52237-sequence guided primer walking of fragment clones and PCR amplicons using an ABI 3130xL Genetic Analyzer (Applied Biosystems, Carlsbad, CA) at the Colorado learn more State University Proteomics and Metabolomics Facility. φX216 Illumina sequencing libraries were prepared using the TruSeq DNA Sample Preparation Kit v2, (Illumina, San Diego, CA), following the manufacturer’s instructions. Phage DNA was fragmented to a range of 300–400 bp using a Covaris acoustic shearing device, (Covaris Inc., Woburn, MA) followed by 3′ adenylation and adapter ligation. Ligation products were purified on an agarose gel and the DNA fragments

enriched via PCR. Fragmented Phage DNA was sequenced by high-throughput Protein kinase N1 Illumina parallel sequencing using 100 bp mate-pair Illumina HiSeq 2000 reversible terminator chemistry. The library was run on 15% of a single lane. Reads were trimmed for quality and de novo short-read genome assembly was performed using the Velvet 1.1.05 sequence assembler algorithms with a hash length of

99 and a final graph with 3 nodes and n50 of 37412 nt [28]. Open reading frames were identified with GeneMark gene prediction software using a viral-optimized Heuristic approach [29]. Putative gene identification was conducted by sequence alignment with φ52237 (GenBank:DQ087285.2) [8] and individual open reading frames queried using the NCBI Basic Alignment Search Tool (BLAST). Genome annotation, mapping, sequence alignments, and comparative analyses were conducted using Gene Construction Kit v3.0 and Geneious Pro 5.4.6 bioinformatics software. The annotation map was created using Adobe Illustrator CS5. The final φX216 genome sequence has been deposited in GenBank under accession # JX681814. Acknowledgements Funding was provided by the Defense Threat Reduction Agency grant W81XWH-07-C0061. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Electronic supplementary material Additional file 1: φX216 host range, word document, Host range of φX216. Table of φX216 host range for 72 B. pseudomallei strains and other Burkholderia species.

Estimates were calculated separately for males and females, and the difference investigated using a bootstrap Wald test. Combined (male and female) associations were also investigated following adjustment for sex. The difference between the effect of buy PLX4032 25(OH)D2 and 25(OH)D3 was calculated from the bootstrap replicate distribution, and the P values using a Wald test. Minimally adjusted analyses (model 1), which were based on seasonally

adjusted 25(OH)D3 levels or 25(OH)D2, were adjusted for sex, age at pQCT scan, and adjusted for 25(OH)D2 and seasonally adjusted 25(OH)D3, respectively. In model 2, we additionally adjusted for loge-transformed fat mass, lean mass and height. In the final model (model 3), we also adjusted for physical activity and social economic factors (maternal or paternal social class, maternal education). Analyses with endosteal circumference were adjusted for periosteal circumference throughout (endosteal adjusted for periosteal circumference). Sensitivity analyses were

BGJ398 in vivo performed based on model 2 by: (a) adjusting for parathyroid hormone (PTH); (b) restricting those with available puberty information and then, in this subgroup, examining the impact of adjusting for pubertal status (tanner stages IV/V versus earlier stages); and (c) restricting those with 25(OH)D assays collected at age 9.9 years. All analyses were conducted using STATA 11.2(College Station, TX, USA), and data is assumed to be missing at random. Results Descriptive analyses There were 1,709 boys and 1,870 girls with pQCT scans (age 15.5 years), and plasma 25(OH)D2 and 25(OH)D3 (age 7.6, 9.9 or 11.8 years; see Fig. 1). Those who were included in the analysis were of higher maternal and paternal social class compared to those who were not. Boys were taller, heavier and had greater lean mass compared to girls, whereas fat mass was higher in girls (Table 1). BMCC, Glutamate dehydrogenase cortical

bone area, periosteal circumference, endosteal circumference and cortical thickness were greater in boys compared to girls, whereas BMDC was higher in girls. 25(OH)D3 levels were slightly higher in boys and 25(OH)D2 levels slightly higher in girls. PTH levels were slightly higher in girls. There was evidence of weak inverse associations between 25(OH)D2 and height LM and FM, which appeared somewhat stronger in girls compared to boys, e.g. P = 0.06 for gender interaction test for association with height (Table 2). There was little association between 25(OH)D3 and height, and LM P > 0.75, and weak evidence of an association with FM P = 0.06. 25(OH)D3 was inversely related to PTH, whereas no association was seen for 25(OH)D2. There was a very weak association between seasonally adjusted 25(OH)D3 and 25(OH)D2, r = −0.0298 P = 0.155, excluding those subjects in whom 25(OH)D2 was below the assay detection limit. Fig.

4 ± 0.6 mV to 8.69 ± 1.3 mV after adding 30 μL NaOH (Table  1). Furthermore, to verify the influence of free MUA in the solution towards the LSPR shift, we found that there was a consistence LSPR shift trend between washed and unwashed GNR-MUA samples. These results demonstrated that the observation of pH-dependent

LSPR shift was apparently related to the changes Proteases inhibitor in the charge of the carboxylic acid groups of MUA bond on GNR instead of free carboxylic groups of MUA (Additional file 1: Figure S3). Figure 4 Reversibility of LSPR shift from GNP, GNP-UDT, and GNP-MUA between pH 2.60 and 11.75. Based on the above observation, subsequent experimental efforts have focused on the reversibility of the system. The titration procedure was repeated several times, going up and down on the pH scale. The LSPR of as-synthesized GNRs and GNR-UDT remains unchanged after the addition of 30 μL NaOH/HNO3 (Figure  4). This result is in good agreement with the result presented above that the LSPR of

as-synthesized GNR and uncharged GNR-UDT was definitely not influenced by pH fluctuation. In comparison, the LSPR shift of GNR-MUA as a function of pH was found to be reversible between pH 11.75 and pH 2.60. Hence, these results indicate that the reversible change to the plasmon of these GNR tethered with MUA shows pH dependence, and this phenomenon demonstrates the utility of our pH nanosensor in a specific range of pH conditions. The LSPR shift Silmitasertib concentration of GNR-MUA is 10.5 nm (821.5 to 832 nm) within the pH range of 6.41 to 8.88 (Figure  5). The S-shaped curve has a linear response range between

pH 6.41 and 7.83. The slope of 5.11 indicated that there was a 5-nm shift of LSPR for each unit change of pH value. This pH-sensing range suggests potential application for pH determination in living-cell organelles such as endosomes and lysosomes, especially for the detection of specific tumor cells for which the cellular pH is within a Carnitine palmitoyltransferase II range between 6.40 and 6.90 [17]. Figure 5 LSPR shift of GNR-MUA ligands as a function of pH in solution. It is well established that the peak wavelength, λ max, of the LSPR is dependent upon the size, shape, and distance between nanoparticles, as well as its dielectric properties and the changes in the effective refractive index (RI) of local surrounding environment including substrate, solvent, and adsorbates [38]. The dependence of LSPR or Fano resonance peak maximum [39] on RI which changes near the metal surface has been utilized in many plasmonic sensing applications. According to the modified equation of the LSPR wavelength shift Δλ max = mΔn(t/l) by Malinsky et al.

The bacterial suspension was incubated with 400 nM diS-C3-(5). ASABF-α was added to the bacterial suspension after the dye uptake was maximal. The maximal increase in fluorescence due to disruption of the cytoplasmic membrane

was recorded. Acknowledgements This work was partly supported by research fellowships of the Japan Society for the Promotion of Science for Young Scientists (to SU). References 1. Brogden KA: Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 2005, 3:238–250.PubMedCrossRef 2. 21 CFR Ch.I (4–1-03 Edition) Food and Drug Administration, HHS.§184.1538 2003. 3. Landman D, Georgescu C, Martin DA, Quale J: Polymyxins revisited. Enzalutamide purchase Clin Microbiol Rev 2008, 21:449–465.PubMedCrossRef 4. Hancock REW, Sahl HG: Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 2006, 24:1151–1157.CrossRef 5. Subbalakshimi C, Sitaram N: Mechanism of antimicrobial action of indolicidin. FEMS Microbiol Lett 1998, 160:91–96.CrossRef 6. Giacometti NVP-LDE225 price A, Cirioni

O, Riva A, Kamysz W, Silvestri C, Nadolski P, Della Vittoria A, Łkasiak J, Scalise G: In vitro activity of aurein 1.2 alone and in combination with antibiotics against gram-positive nosocomial cocci. Antimicrob Agents Chemother 2007, 51:1494–1496.PubMedCrossRef 7. Westerhoff HV, Zasloff M, Rosner JL, Hendler W, De Waal A, Vaz Gomes A, Jongsma PM, Riethorst A, Juretić D: Functional synergism of the magainins PGLa and magainin-2 in Escherichia coli , tumor cells and liposomes. isometheptene Eur J Biochem 1995, 228:257–264.PubMedCrossRef 8. Mor A, Hani K, Nicolas P: The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms. J Biol Chem 1994, 269:31635–31641.PubMed 9. Rosenfeld Y, Barra D, Simmaco M, Shai Y, Mangoni ML: A synergism between temporins toward Gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer. J

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Therefore, it is simplistic and misleading to suggest that there is no data supporting contentions that athletes need more protein in their diet and/or there is no potential ergogenic value of incorporating different types of protein

into the diet. It is the position stand of ISSN that exercising individuals need approximately 1.4 to 2.0 grams of protein per kilogram of bodyweight per day. This is greater than the RDA recommendations for sedentary individuals. According to the current literature we know that the addition of selleck products protein and or BCAA before or after resistance training can increase protein synthesis and gains in lean mass beyond normal adaptation. However, it should be noted that gains have primarily been observed in untrained populations unless the supplement contained other nutrients like creatine Afatinib manufacturer monohydrate [13, 39]. Essential Amino Acids (EAA) Recent studies have indicated that ingesting 3 to 6 g of EAA prior to [105, 106] and/or following exercise stimulates protein synthesis [92, 93, 98–101, 105]. Theoretically, this may enhance gains

in muscle mass during training. To support this theory, a study by Esmarck and colleagues [107] found that ingesting EAA with carbohydrate immediately following resistance exercise promoted significantly greater training adaptations in elderly, untrained men, as compared to waiting until 2-hours after exercise to consume Adenosine the supplement. Although more data is needed, there appears to be strong theoretical rationale and some supportive evidence that EAA supplementation may enhance protein synthesis and training adaptations. Because EAA’s include BCAA’s, it is probable that positive effects on protein synthesis from

EAA ingestion are likely due to the BCAA content [108, 109]. Garlick and Grant [109] infused glucose into growing rats to achieve a concentration of insulin secretion that was insufficient to stimulate protein synthesis by itself. In addition to this, all eight essential amino acids with glucose was infused into another group and then in a third group the investigators only infused the BCAA’s along with the glucose. Compared with the glucose infusion alone, protein synthesis was stimulated equally by the essential amino acids and the BCAAs. This demonstrates that the BCAAs are the key amino acids that stimulate protein synthesis. The ISSN position stand on protein concluded that BCAAs have been shown to acutely stimulate protein synthesis, aid in glycogen resynthesis, delaying the onset of fatigue, and help maintain mental function in aerobic-based exercise.

coli F-18 to occupy a distinct nutritional niche in the streptomycin-treated mouse large intestine. Infect Immun 1996,

64:3497–3503.PubMedCentralPubMed 38. Sweeney NJ, Laux DC, Cohen PS: Escherichia coli F-18 and E. coli K-12 eda mutants do not colonize the streptomycin-treated mouse large intestine. Infect Immun 1996, 64:3504–3511.PubMedCentralPubMed 39. Patra T, Koley H, Ramamurthy T, Ghose AC, Nandy RK: The Entner-Doudoroff pathway is obligatory for gluconate utilization and contributes to the pathogenicity of Vibrio cholerae . J Bacteriol 2012, 194:3377–3385.PubMedCentralPubMedCrossRef Roxadustat mw 40. Izu H, Adachi O, Yamada M: Gene organization and transcriptional regulation of the gntRKU operon involved in gluconate uptake and catabolism of Escherichia coli . J Mol Biol 1997, 267:778–793.PubMedCrossRef 41. Porco A, Peekhaus N, Bausch C, Tong S, Isturiz T, Conway T: Molecular genetic characterization of the Escherichia coli gntT

gene of GntI, the main system for gluconate metabolism. J Bacteriol 1997, 179:1584–1590.PubMedCentralPubMed 42. Peekhaus N, Tong S, Reizer J, Saier MH, Murray E, Conway T: Characterization of a novel transporter family that JQ1 manufacturer includes multiple Escherichia coli gluconate transporters and their homologues. FEMS Microbiol Lett 1997, 147:233–238.PubMedCrossRef 43. Bates Utz C, Nguyen AB, Smalley DJ, Anderson AB, Conway T: GntP is the Escherichia coli fructuronic acid transporter and belongs to the UxuR regulon. J Bacteriol 2004, 186:7690–7696.PubMedCentralPubMedCrossRef 44. Frunzke J, Engels V, Hasenbein S, Gätgens C, Bott M: Co-ordinated regulation of gluconate catabolism and glucose uptake in Corynebacterium glutamicum by two functionally equivalent

transcriptional regulators, GntR1 and GntR2. Mol Microbiol 2008, 67:305–322.PubMedCentralPubMedCrossRef 45. Letek M, Valbuena Resminostat N, Ramos A, Ordóñez E, Gil JA, Mateos LM: Characterization and use of catabolite-repressed promoters from gluconate genes in Corynebacterium glutamicum . J Bacteriol 2006, 188:409–423.PubMedCentralPubMedCrossRef 46. Klein G, Lindner B, Brade H, Raina S: Molecular basis of lipopolysaccharide heterogeneity in Escherichia coli. J Biol Chem 2011, 286:42787–42807.PubMedCentralPubMedCrossRef 47. Mole B, Habibi S, Dangl JL, Grant SR: Gluconate metabolism is required for virulence of the soft-rot pathogen Pectobacterium carotovorum . Mol Plant Microbe Interact 2010, 23:1335–1344.PubMedCrossRef 48. Klein G, Müller-Loennies S, Lindner B, Kobylak N, Brade H, Raina S: Molecular and structural basis of inner core lipopolysaccharide alterations in Escherichia coli: incorporation of glucuronic acid and phosphoethanolamine in the heptose region. J Biol Chem 2013, 288:8111–8127.PubMedCrossRef 49. Mason KM, Bruggeman ME, Munson RS, Bakaletz LO: The non-typeable Haemophilus influenzae Sap transporter provides a mechanism of antimicrobial peptide resistance and SapD-dependent potassium acquisition. Mol Microbiol 2006, 62:1357–1372.

Smith & Macfarlane [1] enumerated amino acid-fermenting colonic bacteria in medium containing peptone, but did not isolate the bacteria concerned, concentrating on bacteria growing on individual or Stickland pairs of amino acids. The latter included mainly Clostridium species, with Peptostreptococcus,

Fusobacterium, Actinomyces, Bacteroides, Megasphaera and Propionibacterium all represented. In the present study, the enrichments resulted in the isolation of several groups of bacteria. None was a HAP species, as all fermented glucose. Thus, the microbial ecology of the rumen and the human colon are fundamentally different in this respect. The species were also different to those isolated by Smith & Macfarlane [1]. Clostridium and Bacteroides were similarly predominant, though RG7422 solubility dmso the species were different. Notably, one of the bacteria enriched

was C. perfringens, which is a pathogen in animal species and man [34, 35]. One might conclude, therefore, that individuals consuming a low-carbohydrate, high-protein weight loss diet would be vulnerable to increased numbers of pathogens in the intestine, as well as the better characterized genotoxic and inflammatory products of amino acid catabolism [2]. Conclusions The metabolism of peptides and amino acids by human faecal bacteria has many parallels Small molecule library with similar metabolism in the rumen, except that the bacteria that grow on these substrates are not specialist

asaccharolytic (HAP) species. Instead, they tend to be pathogens. Thus, the implication is that when protein is the main substrate for intestinal bacteria, not only are the products of protein fermentation toxic, the bacteria enriched by these conditions may be Arachidonate 15-lipoxygenase harmful. Methods Donors These experiments were carried out in compliance with the Helsinki Declaration of Ethical Principles for Medical Research Involving Human Subjects (http://​www.​wma.​net/​en/​30publications/​10policies/​b3/​index.​html). Ethical approval was granted by the North of Scotland Research Ethics Committee and all subjects provided informed signed consent. Fresh faeces were obtained from three omnivorous (O1 – O3) and three vegetarian (V1 – V3) donors. No specific diets were given. O1 and O2 were 33-year-old females, O3 was a 47-year-old female, V1 and V3 were 56- and 26-year-old males, and V2 was a 43-year-old female. None had received antibiotic therapy for 3 months before samples were given. All samples were used fresh. Measurement of ammonia production in faecal suspensions in vitro Faecal samples were diluted 1:10 wet weight in Chen & Russell basal medium [36], the suspension was homogenized in a stomacher, and 10 ml were added, under CO2, to Hungate-type tubes containing 200 mg substrate with or without 10 μl ethanol or 10 μl 5 mM monensin (Sigma, Poole, Dorset, UK) in ethanol.

The weight of p-DMDAAC-CSs (m) could be calculated according to formula (1). The percentage of the grafted p-DMDAAC-CSs and surface grafting density (σ) were calculated according to formula (2). (1) where m 0 is the weight of the CSPBs used for TGA, w 0% is the weight

loss of the CSPBs during the temperature rise from 190°C to 475°C, w 1% is the mass loss of the pure CSs in the same temperature, and w% stood for the mass loss of p-DMDAAC-WL. (2) where Mw is the weight-average molecular weight of p-DMDAAC-CSs, and r is the average size of the CSs. Conductivity tests Conductivity has been tested to compare the promotion of conductive performance of CSs and CSPBs. A 1.5-mg/ml solution of CSs and PLX4032 supplier CSPBs was prepared with water as solvent. The conductivity of CSs and CSPBs water solution was 9.98 and 49.24 μS/cm, respectively.

It can be turned out that the conductivity of CSs increased with the grafting of p-DMDAAC on the surface of the CSs. As shown in Figure 5, the conductive performance of CSPBs decreased with the increase of ionic strength by adding the amount of salt. The reason for this phenomenon was that with the increasing ionic strength, the Debye length diminished [16], inducing the decreasing of the points on the polyelectrolyte brushes. Figure 5 Conductivity of CSPBs in different concentrations of NaCl. Zeta potential and colloidal stability analysis Metabolism inhibitor The zeta potential on the CSs and CSPBs was 11.6 and 42.5 mV, respectively. It showed that polyelectrolyte was successfully grafted on the CSs. And the increase gained in the aspect of zeta potential enabled CSPBs to have better stability in water. As shown in Figure 6, the stratification of CSs appeared 30 s after ultrasonic dispersion, while the CSPBs appeared 1 h later. Figure 6 Dispersibility of (a) CSs and

(b) CSPBs at different times in water. Conclusion Parvulin Surface modification of carbon spheres by grafting p-DMDAAC on their surfaces has been described, and a series of characterization was done. Using FTIR, SEM, conductivity meter, and zeta potential method, the chemical structure, morphology, conductivity, and water dispersibility of the modified CSs were represented. Owing to the p-DMDAAC-CSs, the dispersibility of CSPBs in water has been enhanced obviously, which will expand its application in liquor phase. Because the weight-average molecular weight and surface grafting density can be controlled by adjusting monomer concentration and reaction time, CSPBs with different performances will be obtained; thus, this will further expand its application field. Authors’ information HL is a professor in the School of Printing and Packing at Wuhan University, China. He is a Ph.D. supervisor. His main research interests include packing materials, packing auxiliary materials, and printing materials. QZ, PZ, and YW are studying for a masters degree at Wuhan University.

tularensis strains were richly streaked on MC plates that were incubated in 37°C and 5% CO2 over night. Bacteria were harvested, serially diluted in PBS and 100 μl of a dilution estimated to give approximately 100 colony forming units per plate were evenly spread on MC plates. The plates were incubated at 37°C in an aerobic or microaerobic milieu and the colony size scored after 2, 3, and 6 days of incubation. OxyBlot assay The OxyBlot Protein Oxidation Detection Kit (Chemicon International)

is based on Tigecycline a method for detection of carbonyl groups introduced into proteins by oxidative reactions. The carbonyl groups are derivatized to 2,4-dinitrophenylhydrazone (DNP-hydrazone) by use of 2,4-dinitrophenylhydrazine (DNPH) and can thereafter be detected by immunostaining. The OxyBlot kit was used to compare the amount of oxidized proteins in LVS and ΔmglA grown in an aerobic or a microaerobic milieu. Samples were collected at an OD600 of 0.6-0.7 and the bacteria were lysed using a buffer containing 2 M thiourea, 7 M urea, 4% CHAPS (3-[(3-Cholamidopropyl)dimethylammonio]-1-propanesulfonate), 0.5% ASB-14 (amidosulfobetaine-14), 1.0% DTT, 0.5 × protease inhibitor, and 1% β-mercaptoethanol. The amounts of protein in the samples were determined by use of the Bradford assay (Fermentas, JAK inhibitor St. Leon-Rot, Germany). The assay was carried out according to the manufacturer’s protocol for Standard Bradford assay in microplates.

Equal amounts of proteins were taken from each sample for derivatization and synthesis of negative controls according to the manufacturer’s protocol. Briefly, samples were incubated with 1 × DNPH solution for 15 min at RT to allow derivatization Interleukin-2 receptor of carbonyl-groups to DNP-hydrazone, after which a neutralization solution was added. Negative controls were prepared as the samples with the exception that they were treated with dH2O instead of 1 × DNPH solution, and therefore lack DNP-hydrazone. Negative controls were synthesized in order to ensure the specificity of the antibodies used for detection of DNP-moieties in oxidized proteins. Samples were blotted to PVDF

membranes using a Bio-Dot Microfiltration Apparatus (BioRad), immunostained using a primary Rabbit anti-DNP antibody and a secondary Goat Anti-Rabbit IgG (HRP-conjugated) antibody; and developed with chemiluminescence to visualize the DNP-modifications, as directed by the instructions provided in the OxyBlot Kit. Samples were blotted at a concentration of 2.5 ng of protein in the first well followed by two-fold dilutions thereof. Catalase assay LVS and ΔmglA were cultivated overnight in CDM and thereafter sub-cultured in CDM. When bacteria reached logarithmic growth phase (0.4-0.7 OD600 nm), the OD600 of the cultures were measured and 20-50 μl of culture was withdrawn and transferred to a 96-well UV-clear plate (Greiner Bio-One, Frickenhausen, Germany). To each well, PBS was added to give a final volume of 200 μl.