J Bacteriol 2005, 187:3931–3940.PubMedCrossRef 28. Poggi D, Oliveira de Giuseppe P, Picardeau M: Antibiotic resistance markers for genetic manipulations of Leptospira spp. Appl Environ Microbiol 2010, 76:4882–4885.PubMedCrossRef 29. Bono JL, Elias AF, Kupko JJ, Stevenson B, Tilly K, Rosa P: Efficient targeted mutagenesis in Borrelia burgdorferi . J Bacteriol 2000, 182:2445–2452.PubMedCrossRef 30. Ulixertinib manufacturer Barocchi MA, Ko AI, Reis MG, McDonald KL, Riley LW: Rapid translocation of polarized MDCK cell monolayers by Leptospira interrogans , an invasive but nonintracellular pathogen. Infect Immun 2002,

70:6926–6932.PubMedCrossRef 31. Cao XJ, Dai J, Xu H, et al.: High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans www.selleckchem.com/products/Rapamycin.html . Cell Res 2010, 20:197–210.PubMedCrossRef 32. Haake DA, Mazel MK, McCoy AM, Milward F, Chao G, Matsunaga J, Wagar

EA: Leptospiral outer membrane proteins OmpL1 and LipL41 exhibit synergistic immunoprotection. Infect Immun 1999, 67:6572–6582.PubMed 33. Setubal JC, Reis MG, Matsunaga J, Haake DA: Lipoprotein computational prediction in spirochaetal genomes. Microbiology 2006, 152:113–121.PubMedCrossRef 34. Nougayrède JP, Fernandes PJ, Donnenberg MS: Adhesion of enteropathogenic Escherichia coli to host cells. Cell Microbiol 2003, 5:359–372.PubMedCrossRef 35. Pepe JC, Miller VL: Yersinia enterocolitica

invasin: a primary role in the initiation of infection. Proc Natl Acad Sci USA 1993, 90:6473–6477.PubMedCrossRef 36. Choy HA, Kelley MM, Croda J, Matsunaga J, Babbitt JT, Ko AI, Picardeau M, Haake DA: The multifunctional LigB adhesin binds homeostatic proteins with potential roles in cutaneous infection by pathogenic Leptospira interrogans PRKACG . PLoS One 2011, 6:e16879.PubMedCrossRef 37. Atzingen MV, Barbosa AS, De Brito T, Vasconcellos SA, de Morais ZM, Lima DM, Abreu PA, Nascimento AL: Lsa21, a novel leptospiral protein binding adhesive matrix molecules and present during human infection. BMC Microbiol 2008, 8:70.PubMedCrossRef 38. Barbosa AS, Abreu PA, Neves FO, Atzingen MV, Watanabe MM, Vieira ML, Morais ZM, Vasconcellos SA, Nascimento AL: A newly identified leptospiral adhesin mediates attachment to laminin. Infect Immun 2006, 74:6356–6364.PubMedCrossRef 39. Hauk P, Macedo F, Romero EC, Vasconcellos SA, de Morais ZM, Barbosa AS, Ho PL: In LipL32, the major leptospiral lipoprotein, the C terminus is the primary immunogenic domain and mediates interaction with collagen IV and plasma fibronectin. Infect Immun 2008, 76:2642–2650.PubMedCrossRef 40. Longhi MT, Oliveira TR, Romero EC, Gonçales AP, de Morais ZM, Vasconcellos SA, Nascimento AL: A newly identified protein of Leptospira interrogans mediates binding to laminin. J Med Microbiol 2009, 58:1275–1282.PubMedCrossRef 41.

Reactive oxygen species generated by the phagocyte NADPH oxidase have an essential role in the control of B. pseudomallei infection

in C57BL/6 bone marrow derived macrophages [16]. Type I of all 5 B. pseudomallei isolates tested here had the greatest resistance to H2O2, followed by types II and III, respectively, suggesting that type I has the greatest potential to scavenge or degrade H2O2 molecules. This may explain the finding that type I had the highest replication after uptake by the macrophage cell line. Type III switched to type I or II during culture in medium containing H2O2, indicated that type III had a survival disadvantage under such conditions that required switching to a more H2O2 resistant type. One of the mechanisms by which B. pseudomallei escapes macrophage killing is by repressing inducible nitric Dabrafenib clinical trial oxide synthase (iNOS) by activating the expression of two negative regulators, a suppressor of cytokine signaling 3(SOC3) and cytokione-inducible src homology2-containing protein (CIS) [17]. It is unknown whether there are variation between strains and isogenic morphotypes in the ability to interfere with iNOS induction. However, colony morphology differences did not influence resistance to RNI. B.

pseudomallei is protected Deforolimus solubility dmso from RNI by the production of alkyl hydroperoxide reductase (AhpC) protein and depends on OxyR regulator and a compensatory KatG expression [18]. These mechanisms may not be associated with colony morphology variability. B. pseudomallei survive in the phagolysosome [10] which are acidified environments containing lysozymes, proteins and antimicrobial peptides that destroy pathogen. There was no difference in growth for the 3 isogenic morphotypes of B. pseudomallei

derived from all five isolates at all pH levels tested above 4.0, but a pH of 4.0 was universally bactericidal, suggesting that morphotype switching did not provide a survival advantage against acid conditions. All morphotypes of B. pseudomallei were highly resistance to lysozyme and lactoferrin. Lysozyme functions to dissolve cell walls of bacteria. Lactoferrin is a competitor that works by binding iron and preventing uptake by the bacteria. Common Tolmetin structures for resistance to these factors such as capsule and LPS [8] were present in all isogenic morphotypes [11]. An alternative explanation is that B. pseudomallei may produce a morphotype-independent lysozyme inhibitor that counteracts the action of lysozyme and lactoferrin. Antimicrobial peptides are efficient at killing a broad range of organisms. They are distributed in variety tissues, and in neutrophils and macrophages [12, 13]. All 3 isogenic B. pseudomallei morphotypes were resistant to α-defensin HNP-1 and β-defensin HBD-2, but were susceptible to LL-37. In contrast to sensitivity to H2O2, type III was more resistant than type I or II to LL-37.

We used the PanCGHweb web-tool to find presence/absence of OGs in these strains [37]. Visualizing and identifying presence or absence of a genomic segment Presence or absence of contiguously located genes (i.e. a gene cluster) in a query strain indicates that the whole genomic region encompassing these PD0325901 cell line genes is present or absent in this particular strain. Therefore presence or absence of a genomic segment in a query strain compared to a reference strain was identified. To this end,

probes aligning to a genomic region of interest in a reference strain were identified. The log ratio of probe signals in a query strain to the reference strain was visualized to identify presence or absence of a genomic region in a query strain. Data www.selleckchem.com/products/ABT-263.html pre-processing In PhenoLink, genotype and phenotype data are pre-processed before using them in genotype-phenotype matching analysis.

PhenoLink is based on the Random Forest algorithm [38]. In random forest classification, trees are trained based on random selections of genes and strains, genes with the same occurrence pattern could get different contribution scores [39]. This score is an estimate of how important a gene is to correctly classify a certain strain. Additionally, genes that are either present or absent in (almost) all queried strains have negligible impacts to separate strains of differing phenotypes [40]. Thus we did not use genes with homogeneous occurrence patterns and used only one of the highly correlated genes in further analysis. Prior to classification, phenotypes with continuous measurements were grouped into 3 bins, where each bin represents a different category. Strains that belong to the middle category were not used in genotype-phenotype

matching to improve the classification accuracy. Additionally, in some experiments most of the strains exhibited a single phenotype such as the capability to grow on a certain sugar. Such an imbalance often leads to biased classification. FAD Therefore imbalance in the number of strains per phenotype was decreased by creating 100 bags [22]. Genotype-phenotype matching Genes related to phenotypes were identified using PhenoLink mostly with default parameter settings. To decrease effects of random selection, the same genotype and phenotype data were classified 3 times and only genes consistently relating to phenotypes were selected. Additionally, only genes with a positive contribution score for at least a few (in this study 3) strains of a phenotype were used for further classification, which decreases spurious relations between genes and phenotypes. This iterative removal of genes continued until no more than a few (in this study 5) genes were removed [22].

25 U), MgCl2 (3 mM). Genomic DNA was prepared from single colonies re-suspended in 100 μl of Tris-EDTA buffer (TE, pH 7.5), heated at 95°C for 5 min and centrifuged briefly. The supernatant (2 μl) was used for PCR reactions. The universal primers

forward 27f and reverse 1492r were used for 16S rRNA gene amplification. The primers forward Coprun F2 and reverse Coprun R1 were used for the amplification of the copA gene. The forward primer 5’-GTCGTTAGCTTGCCAACATC-3’ and the reverse primer 5’-CGGAAAGCAAGATGTCGAATCG-3’ [31] were used for chrB gene (chromate resistance) amplification. The forward primer 5’-ACCATCGGCGGCACCTGCGT-3’ and the reverse primer 5’-ACCATCGTCAGGTAGGGGAACAA-3’ were used for merA gene (inorganic mercury resistance) amplification [32]. The forward primers 5’-TCGCCCATATATTTTAGAAC-3’ and the reverse primer 5’-GTCGGGACAGATGCAAAGAAA-3’ were used for merB gene (organic mercury resistance) amplification [32]. DNA amplification learn more of chrB, merA and merB was carried out using the following conditions: 1 cycle of 94°C for 3 min, 30 cycles of 94°C for 1 min, 57°C for 1 min, 72°C for 1 min, plus a final extension at 72°C for 7 min. C. metallidurans MSR33 was used as positive control for copA, chrB, merA and merB genes [31]. PCR products were visualized by agarose gel selleck electrophoresis

followed by staining with GelRed (1:10,000 v/v). 16S rRNA and copA genes sequence analyses The PCR products were visualized by agarose gel electrophoresis. Bands were cut from the gel with a scalpel and DNA was recovery using Zimoclean Gel

DNA Recovery Kit (Irvine, CA, USA). The purified DNA was sequenced directly by an Applied Biosystem 3730XL DNA sequence (Carlsbad, CA, USA), using the primers 27f and 1492r for 16S rRNA gene and Coprun F2 and Coprun R1 for copA gene sequencing, respectively. The nucleotide sequences of 16S rRNA genes were aligned with sequences available in the GenBank (http://​www.​ncbi.​nlm.​nih.​gov/​). The nucleotide sequence of copA gene was translated into a protein sequence using blastx. Then, partial sequences of CopA were aligned with other CopA sequences 3-mercaptopyruvate sulfurtransferase from Cu-resistant bacteria [18]. A phylogenetic analysis was performed to study the evolutionary relationships of the sequences based on the alignments calculated by CLUSTAL W using the default options. The evolutionary history was inferred using the Neighbor-Joining method. Evolutionary analyses were conducted in MEGA 5.05 software [33]. The 16S rRNA gene sequence of strains O12, A32, A55, C21 and O4 were submitted to the EMBL Nucleotide Sequence Database under accession number EMBL:HE608567, EMBL:HE608568, EMBL:HE608569, EMBL:HE608570 and EMBL:HE608571, respectively. The copA gene sequence of strains O12, A32, A55, C21 and O4 were submitted to the EMBL Nucleotide Sequence Database under accession number EMBL:HE716432, EMBL:HE716433, EMBL:HE16434, EMBL:HE16435, EMBL:HE16436, respectively.

For food supply, capsules were provided with grapevine leaves whose petiole

was placed inside an Eppendorf tube containing a nutritive solution [27] and sealed with parafilm to maintain leaf turgor during the experiments. At the end of the mating period, individuals mated with infected S. titanus learn more were fed on sterile sugar diets for different periods (24 to 96 hours), in order to permit the insect’s body colonization by the bacteria acquired during mating. After the incubation periods, both insects and diets were collected and conserved as described above. To control whether the Gfp Asaia transfer really took place by mating, rather than by co-feeding while the two individuals remained in the same capsule, co-housing

trials were set up. Further 12 males and 14 females, after the acquisition of the Gfp-marked bacterium, were placed in Petri dishes together with an uninfected individual of the same sex, under the same conditions of the venereal transfer experiments. After 2 days (without copulation), both the specimens were fed on sterile sugar diets for different periods (24 to 96 hours), like for the other trials. For each co-feeding experiment, other 56 individuals fed on sterile sugar diets were used as donors in trials designed as negative control; similarly, for each venereal transmission experiment, 56 individuals fed on sterile solution were mated with PLX3397 solubility dmso specimens of the opposite sex as negative control (Table 3). After mating of negative control individuals, receiving specimens were maintained singularly on sugar diets for periods varying from 24 to 96 hours to simulate the transmission trials. selleck screening library Quantitative real-time PCR for the Gfp-tagged Asaia Subsequent to the transmission trials, S. titanus individuals and sugar diets for molecular analyses were submitted to total DNA isolation. Nucleic acids extraction was performed by sodium dodecyl sulfate-proteinase K-cethyltrimethyl ammonium bromide treatment [28], which for insects was modified as described in Raddadi et al. [29]. The precipitated DNA was resuspended in 50 µl (insect samples) or in 20 µl (diet samples)

of TE buffer, pH 8 and kept at -20°C until use. Quantitative real-time PCR was performed on a Chromo4 real-time detector (Bio-Rad, Milan, Italy) to measure the presence and concentration of Gfp-tagged Asaia in insects and diets. The reactions were performed with IQTM SYBR® Green Supermix (Bio-Rad), using primers targeting the gfp cassette (GFP540F / GFP875R) [30] and the insect’s 18S rRNA gene (MqFw / MqRv) [31]. The latter were used to normalize the gfp concentration values for the total DNA amount of each sample. To calculate the relative abundance of Gfp-labelled Asaia respect to the total Asaia cells and the whole bacterial community, Asaia-specific and eubacterial primers were used also, according to Favia et al. [6]. To construct standard curves, the gfp gene of Asaia strain SF2.

N Z Med J 1979,90(641):98–100.PubMed 11. Chavalittamrong B, Pidatcha P, Thavisri U: Electrolytes, sugar, calories, osmolarity and pH of beverages and coconut water. Southeast Asian J Trop Med Public Health 1982,13(3):427–31.PubMed 12. Adams W, Bratt DE: Young coconut water for home rehydration in children with mild gastroenteritis. Trop Geogr Med 1992,44(1–2):149–53.PubMed 13. Campbell-Falck D, Thomas T, Falck TM, Tutuo N, Clem K: The intravenous use of coconut water. Am J Emerg Med 2000,18(1):108–11.PubMedCrossRef

14. Mantena SK, Jagadish , Badduri SR, Siripurapu KB, Unnikrishnan MK: In vitro evaluation of antioxidant properties of Cocos nucifera Linn. water. Nahrung 2003,47(2):126–31.PubMedCrossRef 15. Fisher-Wellman K, Bloomer RJ: Acute exercise and oxidative stress: a 30 year history. Dyn Med 2009, 8:1.PubMedCrossRef 16. Saat M, Singh R, Sirisinghe RG, Nawawi M: Rehydration after exercise with fresh young coconut water, carbohydrate-electrolyte KPT-330 cell line beverage and plain water. J Physiol Anthropol Appl Human Sci 2002,21(2):93–104.PubMedCrossRef this website 17. Ismail I, Singh R, Sirisinghe RG: Rehydration with sodium-enriched coconut water

after exercise-induced dehydration. Southeast Asian J Trop Med Public Health 2007,38(4):769–85.PubMed 18. Idárraga AP, Aragón-Vargas LF: Post-exercise rehydration with coconut water [abstract]. Med Sci Sports Exerc 2010,42(5):575. 19. Moran DS, Heled Margaliot M, Shani Y, Laor A, Margaliot S, Bickes E, http://www.selleck.co.jp/products/Rapamycin.html Shapiro Y: Hydration status measurement by radio frequency absorptiometry in young athletes – a new method and preliminary results. Physiol Meas 2004, 25:51–59.PubMedCrossRef 20. Antonio J, Sanders MS, Ehler LA, Uelmen J, Raether JB, Stout JR: Effects of exercise training and amino acid supplementation on body composition and physical performance in untrained women. Nutrition 2000, 16:1043–1046.PubMedCrossRef

21. Cheuvront SN, Ely BR, Kenefick RW, Sawka MN: Biological variation and diagnostic accuracy of dehydration assessment markers. Am J Clin Nutr 2010,92(3):565–73.PubMedCrossRef 22. Wong SH, Chen Y: Effect of a carbohydrate-electrolyte beverage, lemon tea, or water on rehydration during short-term recovery from exercise. Int J Sport Nutr Exerc Metab 2011,21(4):300–10.PubMed 23. Armstrong LE, Maresh CM, Castellani JW, Bergeron MF, Kenefick RW, LaGasse KE, Riebe D: Urinary indices of hydration status. Int J Sport Nutr 1994,4(3):265–79.PubMed 24. Popowski LA, Oppliger RA, Patrick Lambert G, Johnson RF, Kim Johnson A, Gisolf CV: Blood and urinary measures of hydration status during progressive acute dehydration. Med Sci Sports Exerc 2001,33(5):747–53.PubMed 25. Lopez RM, Casa DJ, Jensen KA, Demartini JK, Pagnotta KD, Ruiz RC, Roti MW, Stearns RL, Armstrong LE, Maresh CM: Examining the influence of hydration status on physiological responses and running speed during trail running in the heat with controlled exercise intensity. J Strength Cond Res 2011,25(11):2944–54.

Figure 6 M-H curve of δ-Ni 2 Si NWs measured at different temperatures. The inset is the highlight of the magnetization. Conclusions δ-Ni2Si phase NWs have been successfully synthesized through CVD using a single precursor, NiCl2·6H2O. The influence of the chamber pressure on the product morphology

has been discussed. SEM, TEM, and XRD studies https://www.selleckchem.com/products/Everolimus(RAD001).html were conducted to analyze the growth mechanism and reaction paths. Electrical measurements show that the field emission property of the δ-Ni2Si NWs makes them attractive choices for emitting materials. Magnetic measurements via SQUID at different temperatures show the ferromagnetic property of the δ-Ni2Si NWs, and normalization has been applied to calculate the value of magnetization per unit volume. This work has demonstrated future applications of Ni2Si NWs on biologic cell separation, field emitters, and magnetic storage. Acknowledgments WWW, CLH, and KCL acknowledge the support by National Science Council through grants 100-2628-E-009-023-MY3, 101-2218-E-008-014-MY2, and 100-2628-E-006-025-MY2. References 1. Wu XC, Song WH, Huang WD, Pu MH, Zhao B, Sun YP, Du JJ: Simultaneous growth

of alpha-Si 3 N 4 and beta-SiC nanorods. Mater Res Bull 2001, 36:847–852.CrossRef 2. Morales AM, Lieber CM: A laser ablation method for the synthesis of crystalline semiconductor nanowires. Science 1998, 279:208–211.CrossRef 3. Sun Y, Ndifor-Angwafor NG, Riley DJ, Ashfold MNR: Synthesis and photoluminescence of ultra-thin ZnO nanowire/nanotube

arrays formed by hydrothermal growth. Chem Phys Lett 2006, 431:352–357.CrossRef SCH727965 purchase 4. Dai ZR, Pan ZW, Wang ZL: Novel nanostructures of functional oxides synthesized by thermal evaporation. Adv Funct Mater 2003, 13:9–24.CrossRef 5. Zhang HL, Li F, Liu C, click here Cheng HM: The facile synthesis of nickel silicide nanobelts and nanosheets and their application in electrochemical energy storage. Nanotechnology 2008, 19:165606.CrossRef 6. Maszara WP: Fully silicided metal gates for high-performance CMOS technology: a review. J Electrochem Soc 2005, 152:G550-G555.CrossRef 7. Xiang B, Wang QX, Wang Z, Zhang XZ, Liu LQ, Xu J, Yu DP: Synthesis and field emission properties of TiSi 2 nanowires. Appl Phys Lett 2005, 86:243103.CrossRef 8. Lin HK, Tzeng YF, Wang CH, Tai NH, Lin IN, Lee CY, Chiu HT: Ti 5 Si 3 nanowire and its field emission property. Chem Mater 2008, 20:2429–2431.CrossRef 9. Schmitt AL, Bierman MJ, Schmeisser D, Himpsel FJ, Jin S: Synthesis and properties of single-crystal FeSi nanowires. Nano Lett 2006, 6:1617–1621.CrossRef 10. Schmitt AL, Higgins JM, Jin S: Chemical synthesis and magnetotransport of magnetic semiconducting Fe 1- x Co x Si alloy nanowires. Nano Lett 2008, 8:810–815.CrossRef 11. Seo K, Varadwaj KSK, Mohanty P, Lee S, Jo Y, Jung MH, Kim J, Kim B: Magnetic properties of single-crystalline CoSi nanowires. Nano Lett 2007, 7:1240–1245.CrossRef 12.

In this paper, we present a systematic treatment of Botryosphaeriaceae and its related asexual morph genera based on type specimens sourced from various herbaria and a morphological study of 17 fresh specimens of botryosphaeriaceous taxa from northern Thailand as well as a molecular phylogenetic analysis of sequence

data from four genes. Two monotypic genera and four Ceritinib price new species are introduced, one in Botryosphaeria, one in Phaeobotryosphaeria and two in Aeurswaldia. These taxa are fully described and their taxonomy is discussed. Materials and methods Examination of herbarium material and fresh specimens The type specimens of Auerswaldia, Auerswaldiella, Barriopsis, Botryosphaeria, Leptoguignardia, Melanops, Neodeightonia, Phaeobotryon, Phaeobotryosphaeria, Phyllachorella, Pyrenostigme, Saccharata, Sivanesania, Spencermartinsia and Vestergrenia

were obtained from BPI, K, IMI, LISE, LPS, PREM and S. Fresh material was collected from Chiang Mai, Chiang Rai, Lampang and Phayao provinces in Thailand. Seventeen freshly collected samples were grown on malt extract agar (MEA) and/or potato dextrose agar (PDA). Methods for examining the Z-VAD-FMK datasheet type material and isolation from fresh material were as in Boonmee et al. (2011), Chomnunti et al. (2011) and Liu et al. (2011). To increase the chances of sporulation 3–5 single ascospore cultures were placed around the Petri-dish so that mixing of mycelia

occurred. Observations and photomicrographs were made from material mounted in water using a Nikon ECLIPSE 80i microscope. India ink was added to water mounts to detect the presence of gelatinous sheaths or ascospore appendages. Measurements were CYTH4 made with Tarosoft (R) Image Frame Work (Liu et al. 2010). DNA extraction, PCR amplification and sequencing Fungal isolates were grown on PDA for 1 week at 28 °C in the dark. Genomic DNA was extracted from the fresh mycelium using the Biospin Fungus Genomic DNA Extraction Kit (BioFlux®) following the manufacturer’s protocol (Hangzhou, P.R. China). DNA amplification was performed by polymerase chain reaction (PCR). Primer pairs NS1 and NS4 (White et al. 1990) were used to amplify a region spanning of the nuclear ribosomal SSU gene. LROR and LR5 primer pairs (Vilgalys and Hester 1990) were used to amplify a segment of the large subunit rRNA gene. Primer pairs ITS4 and ITS5 (White et al. 1990) were used to amplify the internal transcribed spacers. Primers EF1–728 F and EF1–986R (Carbone and Kohn 1999) and Bt2a and Bt2b (Glass and Donaldson 1995) were used to amplify and sequence part of the translation elongation factor 1-alpha (EF1-α) gene and part of the β-tubulin gene respectively. Amplification and nucleotide sequencing of the EF1-α and β-tubulin genes were performed as described by Alves et al. (2006, 2008).

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“Background Bacterial intracellular symbiosis (endosymbiosis) is widespread in invertebrates and exhibits a large variety of phenotypes, ranging from mutualism to pathogenesis. Endosymbionts are transmitted vertically for hundreds of host generations and affect the host biology in many ways, including reproduction, physiology and behavior [1–4].