In our experiment, we used a 408-nm excitation wavelength laser

In our experiment, we used a 408-nm excitation wavelength laser. Optical sections were averaged three times to reduce noise. RNase A@C-dots for in

vivo fluorescence imaging Male 4-week-old athymic nude mice were purchased buy LXH254 from Shanghai Slac Laboratory Animal Co. Ltd (Shanghai, China). All experiments that involve animal use were performed in compliance with the relevant laws and institutional guidelines. All animal experiments were approved by the Institutional Animal Care and Use Committee of Shanghai Jiao Tong University (No. SYXK2007-0025). For the establishment of the tumor model, MGC-803 cells were resuspended in PBS, and 2 × 106 cells per site were subcutaneously injected. The tumor nodules had reached a volume of 0.1 to 0.3 cm3 approximately 3 weeks post-injection. For in vivo fluorescence tumor imaging experiments, 100 μl (5 mg/ml) RNase A@C-dot aqueous solution was intratumorally injected into the MGC-803 tumor-bearing mice. Time-course fluorescent images (excitation, 500/20 nm; emission, 600/30 nm; integration time, 5 s) were acquired on a Bruker In-Vivo F PRO imaging system (Bruker, Billerica, MA, USA). Results and

discussion Characterization and properties of RNase A@C-dots TEM images of the as-prepared RNase A@C-dots that were trapped in the dialysis membrane (MW cutoff 1,000) are shown in Figure 1a; the size of the RNase A@C-dots varies mainly within 25 to 45 nm with relatively irregular

morphologies. High-resolution TEM image (Figure 1b, the zoomed-in buy G418 image of the area within the circle in Figure 1a) clearly shows that the particles are actually formed by encapsulating several C-dots within the RNase A film, so we can call them clusters. The clusters can also extremely easily disperse in pure water. In Figure 1c, the average size of C-dot that dispersed out of the dialysis membrane is about 4 nm (Figure 1f) in diameter with nice spherical AICAR manufacturer morphologies (Figure 1d), and the dispersions are also excellent. Lattice spacing of approximately Buspirone HCl 0.23 nm clearly displayed in the high-resolution TEM image (Figure 1d) indicates the (100) facet of graphite [30]. Figure 1 TEM and HR-TEM images, XRD pattern, and size distribution of RNase A@C-dots. (a) TEM image of the as-prepared RNase A@C-dots inside the dialysis membrane after dialyzing against pure water. One typical RNase A@C-dot cluster is labeled with a black circle. (b) High-resolution TEM (HR-TEM) image of one focused area within the black circle. (c) TEM image of the C-dots outside the dialysis membrane. (d) HR-TEM image of one single C-dot. (e) XRD pattern of RNase A@C-dots. (f) Size distribution of C-dots. We can reasonably conclude that during the reaction process accelerated by microwave heating, RNase A capped the different numbers of C-dots that cause the different sizes of particles.

Genomic island PFGI-2 Genomic island 02, or PFGI-2, spans 16 8

Genomic island PFGI-2 Genomic island 02, or PFGI-2, spans 16.8

kb and has an average G+C content of 51.5%. It is flanked by imperfect 51-bp direct repeats, one of which partially overlaps with tRNALeu(6) and probably represents the attB site (see Additional file 10). Although P. fluorescens Pf-5 does not have a type III protein secretion pathway, approximately half of PFGI-2 (i.e. an 8.1-kb LY411575 order DNA segment spanning genes PFL_4977 to PFL_4980) closely resembles a gene cluster found in the exchangeable effector locus (EEL) of a tripartite type III secretion pathogeniCity island (T-PAI) from the plant pathogen P. viridiflava strain ME3.1b [58] (see Additional file 10). Even the presence of a putative phage integrase gene (PFL_4977) (see Additional files 5 and 10) and integration into tRNALeu immediately downstream of the tgt and queA genes is typical of T-PAI islands from P. viridiflava [58] and P. syringae [59]. In addition to T-PAI-like genes, PFGI-2 contains a putative phage-related MvaT-like (PFL_4981) transcriptional regulator, a superfamily II helicase (PFL_4979),

a putative nucleoid-associated protein (PFL_4983), and a putative JIB04 concentration nuclease (PFL_4984). None of the aforementioned homologues of PFGI-2 genes in P. viridiflava have been characterized experimentally to date, making in difficult to deduce the function, if any, of this genome region. It also is possible that PFGI-2 is inactive and simply represents a T-PAI-like buy Erastin remnant anchored in the Pf-5 chromosome. Transposons of P. fluorescens Pf-5 Unlike the genomes of other Pseudomonas spp., that of P. fluorescens Pf-5 is devoid of IS elements and contains only one CDS (PFL_2698) that appears to encode a full-length transposase. Three other transposase-like CDSs (PFL_1553, PFL_3795, and PFL_2699) found in the Pf-5 genome contain frameshifts or encode truncated proteins. PFL_2698 and PFL_2699 encode IS66-like transposases and are found

within a large cluster (PFL_2662 through PFL_2716) of conserved hypothetical genes. Corrupted transposases encoded by PFL_1553 and PFL_3795 belong to the IS5 family and are associated with gene buy VX-770 clusters encoding a putative filamentous hemagglutinin and prophage 06, respectively. Conclusion Recent analyses have revealed that most sequenced bacterial genomes contain prophages formed when temperate bacteriophages integrate into the host genome [60]. In addition to genes encoding phage-related functions, many prophages carry non-essential genes that can dramatically modify the phenotype of the host, allowing it to colonize or survive in new ecological niches [60, 61].

Antimicrob Agents Chemother 1992,36(4):826–829

Antimicrob Agents Chemother 1992,36(4):826–829.PubMed 44. Clements JM, Coignard F, Johnson I, Chandler S, Palan S, Waller A, Wijkmans J, Hunter MG: Antibacterial activities and characterization of novel inhibitors of LpxC. Antimicrob Agents Chemother 2002,46(6):1793–1799.CrossRefPubMed 45. Reuter G, Janvilisri #Mdivi1 ic50 randurls[1|1|,|CHEM1|]# T, Venter H, Shahi S, Balakrishnan L, van Veen HW: The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities. J Biol Chem 2003,278(37):35193–35198.CrossRefPubMed 46. Ghanei H, Abeyrathne PD, Lam JS: Biochemical characterization of MsbA from Pseudomonas

aeruginosa. J Biol Chem 2007,282(37):26939–26947.CrossRefPubMed 47. Waidner B, Greiner S, Odenbreit S, Kavermann H, Velayudhan J, Stahler F, Guhl J, Bisse E, van Vliet AH, Andrews SC, et al.: Essential role of ferritin Pfr in Helicobacter pylori iron metabolism and gastric colonization. Infect Immun 2002,70(7):3923–3929.CrossRefPubMed 48. Bleumink-Pluym NM, Verschoor F, Gaastra W, Zeijst BA, Fry BN: A novel approach for the construction of a Campylobacter mutant library. Microbiology 1999,145(Pt 8):2145–2151.CrossRefPubMed 49. Kim JS, Chang

JH, Chung SI, Yum JS: Molecular cloning and characterization of the Helicobacter pylori fliD gene, an essential factor in flagellar structure and motility. J Bacteriol 1999,181(22):6969–6976.PubMed 50. Ryan KA, Karim N, Worku M, Penn CW, O’Toole PW: Helicobacter pylori flagellar hook-filament transition is controlled by a FliK

functional homolog encoded by the gene HP0906. J Bacteriol 2005,187(16):5742–5750.CrossRefPubMed 51. Pflock M, Bathon M, Schar J, Muller Tideglusib clinical trial S, Mollenkopf H, Meyer TF, Beier D: The orphan response regulator HP1021 of Helicobacter pylori regulates transcription of a gene cluster presumably involved in acetone metabolism. J Bacteriol 2007,189(6):2339–2349.CrossRefPubMed 52. Hughes NJ, Clayton CL, Chalk PA, Kelly DJ: Helicobacter pylori porCDAB and oorDABC genes encode distinct pyruvate:flavodoxin and 2-oxoglutarate:acceptor oxidoreductases which mediate electron transport to NADP. J Bacteriol 1998,180(5):1119–1128.PubMed Authors’ contributions HC, TL, and JW conceived and designed the experiments. HC carried out the experiments, analyzed the data, and drafted the manuscript. Org 27569 JY provided clinical isolate strains. TL and JW modified the manuscript. All the authors have read and approved the final manuscript.”
“Background Genome sequencing of diverse bacterial species has revealed widespread distribution of conserved gene products with as-yet unknown functions. Among these are a family of small proteins with approximate molecular masses of 12 kDa, which have been variously classed as “”domain of unknown function”" (DUF) 149, Pfam 2575 and COG-0718 [1]. Such genes have been identified in a wide variety of bacterial phyla, a list that includes many significant pathogens of humans, domestic animals and plants (Fig. 1).

Based on these observations, Warimwe et al conclude that two sub

Based on these observations, Warimwe et al. conclude that two subsets of A-like var genes must exist that cause disease by very different means. They hypothesize

that the subset associated with impaired consciousness causes severe disease through tissue specific sequestration, while the subset associated with rosetting causes RD and sometimes also IC through a non-tissue-specific mechanism; however, they SP600125 were unable to identify a genetic PX-478 chemical structure marker that could distinguish these two subsets of var genes [10]. One possibility is that the var DBLα tag does not contain the differentiating factor, but another possibility is that the methods used by Warimwe et al. to distinguish different types of tag sequences did not fully capture all the functionally relevant genetic variation within the tag. Here we address whether it is possible to capture more of the phenotypically relevant genetic diversity within a var DBLα tag by taking advantage of its homology block architecture. We hypothesize that since HBs are the units of sequence conservation and the means by which diversity is generated in var genes (i.e. through recombination), they may reflect functionally relevant sequence diversity that correlates

with disease phenotype. To test this hypothesis, we reanalyzed the data originally analyzed by Warimwe et al. [9, 10], looking for correlations between the expression of particular homology blocks and the occurrence of particular disease

phenotypes. We find that a generic set of HBs, which were defined Selleckchem Berzosertib using only a few geographically distinct Cyclin-dependent kinase 3 isolates [8], are capable of describing the variation observed at this local scale in Kenya. When we test for genotype-phenotype relationships, we find that those described by HBs are statistically stronger than those described previously. We further show that a principal component analysis (PCA) of HB expression rate profiles across isolates can break down HB variation in a way that is useful for generating high quality genotype-phenotype models. Methods Homology block nomenclature The DBLα homology blocks discussed here are those described in Rask et al. [8]. These are distinct from the DBLα “homology blocks” of Smith et al. [25] and the DBLα “blocks” of Bull et al. [12] both in definition, and for the most part, in practice. Therefore, wherever we refer to homology blocks (HBs) below, we mean those of Rask et al., and we use their system of numbering to refer to particular HBs as well. Data and HB assessment of sequences The expressed sequences and the clinical data for 250 isolates (217 symptomatic, 33 asymptomatic) were obtained from the online supplementary information of [10]. The genomic sequences for 53 isolates were obtained from EMBL using the reference numbers in [9] for the genomic sequences: FN592662–FN594512.

Moreover, the diameters and charges of metal ions may have great

Moreover, the diameters and charges of metal ions may have great influence on the sizes and properties of nanoscale GO which will be further confirmed by subsequent work. Figure 5 C 1s XPS of GO and nanoscale GO sheets. (a) GO before cutting reaction; (b) nanoscale GO JSH-23 mw after cutting reaction. The peaks 1, 2, 3, and 4 correspond to C=C/C-C in aromatic rings, C-O (epoxy and alkoxy), C=O, and COOH groups, respectively. Conclusions In summary, we have demonstrated

a very simple strategy to obtain nanoscale GO pieces using metal ions as oxidation reagent at mild condition. Without being heated or treated ultrasonically, two kinds of nanoscale GO pieces: GO pieces and nanoparticle-coated GO piece composites, are obtained. Based on systematic investigations of nanoscale GO piece formation by the addition NCT-501 nmr of Ag+ ions as a tailoring reagent, a probable mechanism is suggested to explain the formation of nanoscale GO pieces, which can be mainly attributed to interaction of metal ions (Ag+, Co2+, Ni2+, etc.) with the reducing groups (e.g., epoxy groups) on the basal plane of other GO sheets. Obviously,

in this progress a large-scale GO acts with dual functions, as a reducing reagent and a nucleation site of metal or metal oxide nanoparticles. This work provides a good way or chance to fabricate nanoscale GO pieces and GO composites in water solution and more widely apply in nanoelectronic devices, biosensors, and biomedicine. Acknowledgements This work is HDAC inhibitor supported by the National Key Basic Research Program (973 Project; nos. 2010CB933901 and 2011CB933100) and National Natural Scientific Fund (nos. 31170961, 81101169, 20803040, 81028009, and 51102258). Electronic supplementary material Additional file 1: Supporting information. The file contains Figures S1, S2, and S3 and a discussion of the conductive testing by conductive atomic force microscopy. (PDF 4 MB) References 1. Novoselov K, Geim A, Morozov S, Jiang D, Zhang Y, selleck chemical Dubonos S, Grigorieva I, Firsov A: Electric field effect in atomically thin carbon films.

Science 2004,306(5696):666–669.CrossRef 2. Allen MJ, Tung VC, Kaner RB: Honeycomb carbon: a review of graphene. Chem Rev 2010,110(1):132.CrossRef 3. Lu ZX, Zhang LM, Deng Y, Li S, He NY: Graphene oxide for rapid microRNA detection. Nanoscale 2012,4(19):5840–5842.CrossRef 4. Zhang LM, Wang ZL, Lu ZX, Shen H, Huang J, Zhao QH, Liu M, He NY, Zhang ZJ: PEGylated reduced graphene oxide as a superior ssRNA delivery system. J Mater Chem B 2013,1(6):749–755.CrossRef 5. Zhang LM, Xing YD, He NY, Zhang Y, Lu ZX, Zhang JP, Zhang ZJ: Preparation of graphene quantum dots for bioimaging application. J Nanosci Nanotechnol 2012,12(3):2924–2928.CrossRef 6. Geim AK, Novoselov KS: The rise of graphene. Nat Mater 2007,6(3):183–191.CrossRef 7.

The sharp peaks in the XRD profiles indicate the high crystallini

The sharp peaks in the XRD profiles indicate the high crystallinity of the PbTe sample. However, the XRD profile for PbTe-1 sample shows two weak peaks on either side of the (220) peak, which can be attributed to the presence of some elemental Te [22]. The residual Te indicates that the synthesis in ethanol at relatively low temperature (140°C) is an incomplete reaction. The results indicate that if ethanol is used as the solvent, a high reaction temperature is needed to promote a

complete reaction and achieve high-purity PbTe (see the XRD pattern labeled PbTe-3 in Figure  1a). Furthermore, if a water/glycerol mixture is selleck chemicals llc utilized check details as the solvent, pure phase of PbTe can be formed at either a low temperature of 140°C (see the XRD pattern labeled PbTe-2 in Figure  1a) or a high temperature of 200°C (see the XRD pattern labeled PbTe-4 in Figure  1a). It is clear that solvent of a water/glycerol mixture facilitates the reaction. Because only water/glycerol mixture yields a pure phase of PbTe at all synthesis conditions including lower temperature (140°C) synthesis, our all indium-doped samples were prepared in water/glycerol solution at 140°C for 24 h, which are the same conditions used for synthesizing undoped sample PbTe-2. Figure 1 XRD patterns of undoped and In-doped PbTe samples. (a) XRD patterns of the

as-prepared undoped PbTe samples synthesized without surfactants for 24 h: PbTe-1 at 140°C in ethanol solution, PbTe-2 at 140°C in water/glycerol solution, PFT�� manufacturer PbTe-3 at 200°C in ethanol, and PbTe-4 at 200°C in water/glycerol solution. (b) XRD pattern of In-doped PbTe samples synthesized at 140°C for 24 h: In005PbTe, In01PbTe, In015PbTe, and In02PbTe synthesized in water/glycerol solution. Figure  1b represents the XRD patterns of In-doped PbTe (In005PbTe, In01PbTe, In015PbTe, and DOK2 In02PbTe) synthesized at 140°C for 24 h in water/glycerol solution. All the

diffraction peaks belong to the same face-centered cubic structure as that of PbTe and the very sharp peaks indicating the high crystallinity of the as-synthesized In-doped PbTe samples. XRD patterns do not show any peaks corresponding to elemental indium, indicating that indium is likely doped in PbTe. Lattice constants of undoped (PbTe-2) and indium-doped samples were calculated from the respective XRD profiles using Bragg’s law and were tabulated in Table  1. As indium atoms are smaller in diameter than Pb atoms, lattice constants of the In-doped PbTe are expected to decrease. However, the lattice constants for undoped and all indium-doped PbTe samples are almost the same (average value approximately 6.434 Å) which is in agreement with the reported value for undoped cubic PbTe (6.454 Å, JCPDS: 78-1905). Figure  2 shows the variation of lattice constant of our indium-doped PbTe samples with different molar fractions of indium doping prepared at 140°C for 24 h in water/glycerol solution.

[32] Our isolates were from over nine food types and only those

[32]. Our isolates were from over nine food types and only those from chicken and pork had sufficient numbers for comparison of clonal diversity between food types. There were 48 samples each from chicken and pork. In both food types, ST9 was predominant with 11 and 30 isolates in chicken and pork respectively. Genetic diversity is higher from chicken samples as measured by Simpson’s index of diversity Selleckchem S63845 with 0.906 and 0.722 for chicken and pork respectively. Population structure and recombination of L. monocytogenes Many studies

have shown that L. monocytogenes can be divided into three lineages [20, 21]. Lineage I includes isolates of serotypes 4b, 1/2b, 3b, 4d and 4e, containing all food-borne-epidemic isolates as well as isolates from sporadic cases in humans and animals. Lineage II includes isolates of serotypes 1/2a, 1/2c, 3a and 3c, containing both human and animal isolates, but is seldom associated with food-borne epidemics and predominantly isolated from food products. Lineage III are mostly serotypes 4a and 4c and is predominantly isolated from animals [20, 33]. All our isolates can be allocated into one of the three lineages. The majority of our isolates (154 out of 212, 72.6%) including the 60 isolates of ST9 (the most frequent ST in China) belonged to lineage II since learn more our isolates

were from food sources. Fifty six isolates (26.4%) belonged to lineage I while only two isolates, both being ST299 belonged to lineage III. We used Pembrolizumab the counting method used by Feil et al. [34] to determine the ratio of recombination

to mutation per locus. A single allelic difference between STs within a clonal complex was attributed to either mutation if the difference was a single base or recombination otherwise. We found that alleles are three times more Selleck GW786034 likely to change by mutation than by recombination (r/m = 0.306). This estimate is similar to that (r/m = 0.197) reported by Ragon et al. [23]. Interestingly, five of the eleven recombination events observed were in the same gene (abcZ), three in CC9, one in CC87 and one in CC155. A possible explanation for the high frequency of recombination in abcZ is positive selection. However Ragon et al. [23] showed that the ratio of non-synonymous/synonymous substitution rate (Ka/Ks) of abcZ was 0.014 suggesting that abcZ was not under positive selection. An alternative explanation is that abcZ is linked to a nearby gene that is under positive selection and has undergone recombination by hitch-hiking. This scenario has been observed to have occurred in genes around the O antigen encoding locus in E. coli and other species [26]. Examination of sequences 30 kb up and down stream of abcZ based on the genome sequence of isolate EGD-e did not identify a gene or gene cluster that is likely to be under positive selection.

The rats were exposed to the nanomaterial suspension by intratrac

The rats were exposed to the nanomaterial suspension by intratracheal instillation once every 2 days for 5 weeks. The group of corn oil-instilled rats served as controls. After removal from the inhalation anesthetic, the rats recovered and were active within 10 min. The rats were divided into seven groups randomly by weight, including low-and high-dose groups of the three Savolitinib in vitro nanomaterials, and a control group. Histopathological evaluation The middle of the left lungs was embedded in paraffin and thin-sectioned coronally; then, sections

were stained with hematoxylin-eosin and examined by light microscopy. Preparation of BALF and detection Twenty-four hours after the last instillation, rats were anesthetized with ether, bled from the femoral artery and sacrificed by cervical Wortmannin decapitation. The lung and trachea were exposed by dissection, and then the left lung was temporarily clamped. The right lung was lavaged with 6 mL of warm normal saline; then, the recovered BALF were centrifuged at 400 × g for 10 min. The concentrations of lactate dehydrogenase (LDH), total antioxidant

capacity (T-AOC), superoxide dismutase (SOD), and malondialdehyde eFT-508 research buy (MDA) in BALF were analyzed using biochemical analysis kits (Shangbo, Beijing, China). The reactions were measured using a UV/Vis spectrometer (UNICAM UV2, ATI-Unicam, Cambridge, UK). The levels of interleukin-1 (IL-1), interleukin-6 (IL-6), and tumor necrosis

factor alpha (TNF-α) in lung homogenates were analyzed using enzyme-linked immunosorbent assay (ELISA) kits (Shangbo). The reactions were measured using an ELISA reader. Comparative proteomics analysis The left lungs of rats were excised, immediately cooled in ice, and homogenized in a Teflon-glass homogenizer. Then, the homogenates were centrifuged at 700 × g for 15 min. Homogenized lung tissue of 40 to 100 mg was placed in 2 mL of lysis buffer containing 8 mol · L−1 urea, 4% CHAPS, 40 mmol · L−1 BCKDHB Tris, 65 mmol · L−1 DDT, and 1 mmol · L−1 PMSF and then centrifuged for 20 min at 12,000 rpm after being kept for 1 h at room temperature. Samples were stored in aliquots at −80°C. Protein determination was carried out according to the Bradford assay. Two-dimensional electrophoresis First-dimension isoelectric focusing on immobilized pH gradient One milligram of protein sample, 7 μL of DTT (1 mol · L−1), and 1.75 μL of IPG buffer (20 mmol · L−1) were solubilized in 350 μL of rehydration solution containing 8 mol · L−1 urea, 2% CHAPS, and a trace of bromophenol blue. This solution was pipetted into each 18-cm pH 3-10 strip holder. The strip holder was positioned on the IPGphor™ 3 isoelectric focusing system (Amersham Pharmacia, Little Chalfont, UK). Rehydration and isoelectric focusing (IEF) were carried out at 20°C.

PubMedCrossRef 12 De Freitas LA, Mbow LM, Estay M, Bleyenberg JA

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to sequence typing in Streptococcus pneumoniae causing invasive disease in Chinese children. Eur J Clin Microbiol Infect Dis 2011,31(3):217–223.PubMedCrossRef 39. Vestrheim DF, Hoiby EA, Aaberge IS, Caugant DA: Phenotypic and genotypic characterization of Streptococcus pneumoniae strains colonizing children attending day-care centers in Norway. J Clin Microbiol 2008,46(8):2508–2518.PubMedCrossRef 40. Shin J, Baek JY, Kim SH, Song JH, Ko KS: Predominance of ST320 among Streptococcus pneumoniae serotype 19A isolates from 10 Asian countries. J Antimicrob Chemother 2011,66(5):1001–1004.PubMedCrossRef 41. Ko KS, Song CFTR inhibitor JH: Evolution of erythromycin-resistant Streptococcus

pneumoniae from Asian countries that contains erm(B) and mef(A) genes. J Infect BEZ235 Dis 2004,190(4):739–747.PubMedCrossRef 42. McGee L, McDougal L, Zhou J, Spratt BG, Tenover FC, George R, Hakenbeck R, Hryniewicz W, Lefévre JC, Tomasz A, et al.: Nomenclature of major antimicrobial-resistant clones of Streptococcus pneumoniae defined by the pneumococcal molecular epidemiology network. J Clin Microbiol 2001,39(7):2565–2571.PubMedCrossRef Authors’ contributions LZ and XM conducted the laboratory work, performed the analysis, wrote the draft, and are the co-first authors for the same contributions of this study. WG, KY, AS, and SY provided the bacterial isolates and laboratory supplies. YY planned the study. All

authors read and approved the final manuscript.”
“Background In the oral cavity, bacteria encounter many different stress factors. Shear-forces Molecular motor and high flow rates of saliva dominate on exposed surfaces, while bacteria colonizing the gingival crevices and/or subgingival pockets have to contend and withstand with the host’s immune response. As in most other environments, bacteria form VX-680 purchase biofilms as protection from these harsh conditions [1]. The bacterial community colonizing the oral cavity is highly complex and varies considerably between different individuals. According to current reports, 600 to 700 established species and likely several thousand only partially cultivable taxa can be detected [2]. However, this consortium does not pose a threat to a healthy individual. It even has a protective function by preventing the establishment or predominance of harmful organisms [3]. Several factors like imbalanced nutrition, smoking, diabetes, emotional stress, or genetic predisposition [4] can lead to changes in the composition of this subgingival community, leading to a loss of the natural ecological balance. Potentially pathogenic species may increase in numbers, starting to cause persistent infections of host tissues that are capable to cause not only tooth loss and bone resorption but also can spread out to extra-oral sites and become systemic [5].