“
“Malaghan Institute of Medical Research, Wellington, New Zealand Antiretroviral therapy (ART) suppresses HIV viraemia, thereby reducing

the antigenic drive for T cells to proliferate. Accordingly, selected HIV-specific T-cell responses have been described to contract within weeks of ART initiation. Here, we sought to investigate whether these findings apply to the entire repertoire of HIV-specific T cells. Using interferon (IFN)-γ enzyme linked immuno spot (ELISpot), we performed retrospective 2-year proteome-wide monitoring of HIV-specific T cells in 17 individuals with undetectable viral loads during ART. The sample pool for each study subject consisted of one pre-ART time-point and at

least two time-points after initiation of therapy. Peripheral pools of HIV-specific T cells decreased nonsignificantly within the first 2 years under ART in our cohort Fludarabine of patients, in terms of both breadth and magnitude. However, in most cases, the seeming decrease masked ongoing expansion of individual LBH589 price HIV-specific T-cell responses. We detected synchronous contraction and expansion of T-cell responses – with different peptide specificities – in 12 out of 17 study participants during follow-up. Importantly, the observed expansions and contractions of individual HIV-specific T-cell responses reached similar ranges, supporting the biological relevance of our findings. We conclude that successful ART enables both contraction and expansion of HIV-specific T-cell responses. Etofibrate Our results should prompt a renewed interest in HIV-specific T-cell dynamics under ART, in particular to elucidate the mechanisms that uncouple, to some extent, particular HIV-specific

T-cell responses from variations in circulating antigen load and functionally characterize expanding/contracting T-cell populations beyond IFN-γ secretion. Assuming that expanding HIV-specific T-cell responses under ART are protective and functional, harnessing those mechanisms may provide novel opportunities for assisting viral control in chronically infected individuals. “
“Amino acid insertions in the protease gene have been reported rarely, and mainly in patients receiving protease inhibitors (PIs). The aim of the study was to assess the long-term viro-immunological follow-up of HIV-infected patients harbouring virus with protease insertions. Cases of virus exhibiting protease insertions were identified in routine resistance genotyping tests. Therapeutic, immunological and virological data were retrospectively collected. Eleven patients harbouring virus with a protease gene insertion were detected (prevalence 0.24%), including three PI-naïve patients. The insertions were mainly located between codons 33 and 39 and associated with surrounding mutations (M36I/L and R41K). The three PI-naïve patients were infected with an HIV-1 non-B subtype.

Nonnucleos(t)ide HIV-1 reverse transcriptase inhibitor (NNRTI)-based combination antiretroviral therapies have been gaining popularity over protease inhibitor antiretroviral therapy, and have become preferred therapy options for treatment-naïve individuals as per treatment guideline recommendations [4]. In addition, recent publications have reported increased adherence to therapeutic regimens with the use of once-daily (qd) dosing [5-7]. The antiviral activity and safety of the NNRTI nevirapine www.selleckchem.com/products/VX-770.html (NVP) are well established [8-11]. NVP is a potent NNRTI with

high bioavailability, a long half-life and no effect of food on its absorption [12]. It is available as an immediate release (IR) formulation, which is administered as 200 mg twice daily (bid). qd dosing learn more will further simplify the administration of NVP and has the potential to improve adherence, which in turn should enhance long-term efficacy. A newly developed 400 mg NVP extended release formulation (NVP XR) administered qd has recently been investigated and found to be well tolerated and to have high and comparable efficacy

to NVP immediate release (NVP IR) 200 mg bid in treatment-naïve individuals [13]. The current study investigated the efficacy, defined as continued virological response, at 24 weeks of follow-up, and the safety and tolerability of switching treatment-experienced patients from NVP IR bid to NVP XR qd. This trial is a multinational, open-label, Phase IIIb, randomized, parallel-group study to evaluate the efficacy and safety of switching HIV-1-infected patients, successfully treated with an NVP IR 200 mg bid regimen, to NVP XR 400 mg qd, in comparison to remaining on NVP IR 200 mg bid. The trial is continuing to collect data up to 144 weeks of follow-up. The study population is composed of adult (age ≥ 18 years) patients who were receiving NVP IR with a fixed-dose combination background therapy of lamivudine/abacavir (3TC + ABC), tenofovir/emtricitabine (TDF + FTC), or lamivudine/zidovudine (3TC + ZDV), or their this website individual components, for a preceding

minimum of 18 weeks, with undetectable (< 50 HIV-1 RNA copies/mL) HIV-1 viral load (VL) in the previous 1–4 months and at screening. Patients provided written consent and the trial (NCT00819052; TRANxITION) was conducted in accordance with good clinical practice and the ethical principles of the Declaration of Helsinki (1996 version) [14]. Trial protocol, amendments, informed consent and subject information were reviewed by the central or local institutional review board and independent ethics committees of the participating institutions. Patients were stratified according to their background therapy and randomized within each stratum in a 2:1 ratio to either switch to NVP XR 400 mg qd or continue with NVP IR 200 mg bid. All data were recorded using electronic data capture methods.

Nonnucleos(t)ide HIV-1 reverse transcriptase inhibitor (NNRTI)-based combination antiretroviral therapies have been gaining popularity over protease inhibitor antiretroviral therapy, and have become preferred therapy options for treatment-naïve individuals as per treatment guideline recommendations [4]. In addition, recent publications have reported increased adherence to therapeutic regimens with the use of once-daily (qd) dosing [5-7]. The antiviral activity and safety of the NNRTI nevirapine Crizotinib price (NVP) are well established [8-11]. NVP is a potent NNRTI with

high bioavailability, a long half-life and no effect of food on its absorption [12]. It is available as an immediate release (IR) formulation, which is administered as 200 mg twice daily (bid). qd dosing Paclitaxel will further simplify the administration of NVP and has the potential to improve adherence, which in turn should enhance long-term efficacy. A newly developed 400 mg NVP extended release formulation (NVP XR) administered qd has recently been investigated and found to be well tolerated and to have high and comparable efficacy

to NVP immediate release (NVP IR) 200 mg bid in treatment-naïve individuals [13]. The current study investigated the efficacy, defined as continued virological response, at 24 weeks of follow-up, and the safety and tolerability of switching treatment-experienced patients from NVP IR bid to NVP XR qd. This trial is a multinational, open-label, Phase IIIb, randomized, parallel-group study to evaluate the efficacy and safety of switching HIV-1-infected patients, successfully treated with an NVP IR 200 mg bid regimen, to NVP XR 400 mg qd, in comparison to remaining on NVP IR 200 mg bid. The trial is continuing to collect data up to 144 weeks of follow-up. The study population is composed of adult (age ≥ 18 years) patients who were receiving NVP IR with a fixed-dose combination background therapy of lamivudine/abacavir (3TC + ABC), tenofovir/emtricitabine (TDF + FTC), or lamivudine/zidovudine (3TC + ZDV), or their click here individual components, for a preceding

minimum of 18 weeks, with undetectable (< 50 HIV-1 RNA copies/mL) HIV-1 viral load (VL) in the previous 1–4 months and at screening. Patients provided written consent and the trial (NCT00819052; TRANxITION) was conducted in accordance with good clinical practice and the ethical principles of the Declaration of Helsinki (1996 version) [14]. Trial protocol, amendments, informed consent and subject information were reviewed by the central or local institutional review board and independent ethics committees of the participating institutions. Patients were stratified according to their background therapy and randomized within each stratum in a 2:1 ratio to either switch to NVP XR 400 mg qd or continue with NVP IR 200 mg bid. All data were recorded using electronic data capture methods.

Genomic DNA was isolated from R16-18d and the sequence of the 16s rRNA gene was determined to be identical to the sequence from NCTC 8325-4 and RRSA16 as described above.

MICs were determined on microdilution plates according to Wiegand et al. (2008) using CAMHB2 as the growth media. Sodium chloride was added to a final concentration of 2% (w/v) when oxacillin was tested. BSA (0.02% w/v) was added to media when vancomycin, ramoplanin or nisin was tested to prevent peptide adhesion to polystyrene. Doubling times were calculated as described (Cui et al., 2003), with tryptic soy broth (TSB) cultures growing APO866 mw at 37 °C with aeration in the exponential phase [Eqn. (1)], where t1 and t2 are the times of measurement: (1)

Staphylococcus aureus cultures were grown in TSB supplemented with 0.02% BSA (TSB+BSA) at 37 °C with shaking at 200 r.p.m. to OD620 nm≈0.4 and were then treated with an antibiotic. The cultures were then incubated at 37 °C with shaking at 200 r.p.m. Samples were removed periodically for OD measurements and viable counting. Staphylococcus aureus cultures were grown in TSB+BSA at 37 °C with aeration to an OD620 nm of ≈0.7. Samples were removed, pelleted and resuspended in 4% glutaraldehyde. The pellets were washed twice in 0.1 M sodium cacodylate buffer containing 7.5% sucrose and pre-embedded in 1% agar. The samples were washed twice with selleck kinase inhibitor 0.1 M sodium cacodylate buffer containing 7.5% sucrose and postfixed in 1.0% osmium

tetroxide 4-Aminobutyrate aminotransferase in 0.15 M sodium cacodylate buffer. Samples were washed for 10 min twice in 0.11 M veronal acetate buffer. Samples were then dehydrated in an ascending ethanol series and embedded in Epon resin. Sections were cut at 80 nm on a Reichert Ultracut S ultramicrotome and mounted on copper rhodium 200 mesh 3 mm grids. Samples were stained with uranyl acetate for 30 min, rinsed three times in distilled water, stained with Reynold’s lead citrate stain prepared as described by Venable & Coggeshall (1965) for 5 min and rinsed three times in distilled water. Samples were viewed using a Philips/FEI CM12 transmission electron microscope at 80 kV. Cell wall thickness was calculated as described elsewhere (Cui et al., 2000). Twenty radial lines arranged regularly at angles of 18° were placed over the center of images of equatorially cut cells at a final magnification of × 35 000 and the thickness of the cell wall was measured from at least 10 different points. The thickness of the cell walls of 20 cells from each strain was measured. Results are reported as means±SD. The diameter of the 20 cells from each strain was also measured using 20 radial lines arranged regularly at angles of 18° and placed over the center of equatorially cut cells; the results were reported as means±SD. The statistical significance of the data was evaluated using a Student’s t-test.

3). Identification and characterization of several structural proteins of both the inner basal layer(s) and the external DNA Damage inhibitor projections of the exosporium has in recent years increased our knowledge on this poorly understood component of the bacterial spore (Charlton et al., 1999; Sylvestre et al., 2002; Steichen et al., 2003; Todd et al., 2003; Redmond et al., 2004; Fazzini et al., 2010; Terry et al., 2011; Thompson et al., 2011a, b). The current study identified BC1245 as a spore-specific protein. Bc1245 is highly conserved in members of the B. cereus group (B. anthracis, B. cereus, B. thuringiensis and B. weihenstephanensis)

supportive of an important function of the gene (and possibly its gene product) in this group of bacteria. Members of the B. cereus

group are known to have an exosporium as the outermost part of their spores, and as bc1245 was present in this group of bacteria while other Bacilli species such as B. subtilis lack the gene, we wanted to investigate whether bc1245 encode an exosporium protein. In silico analysis find more indicated that the bc1245 promotor was under control of the mother cell–specific sigma factor K (σK), which regulon in B. subtilis includes a series of genes encoding outer spore structural components such as coat proteins (Errington, 1993; Haldenwang, 1995). Real-time PCR revealed that bc1245 is transcribed late in sporulation (at the onset of phase-bright spores) and expressed at the same time as high expression of sigG and sigK. Although expression is declining, sigE and sigF are also expressed in the time frame of bc1245 expression. Further studies on expression of bc1245 in sigma factor-mutant strains and determination of the transcription start will determine the sigma factor-regulating expression of bc1245. The combination, however, of the prediction of a sigma factor K-dependent promotor and simultaneous expression with sigK make it plausible that bc1245

might encode a structural outer spore protein in the σK regulon. A recent study describing a novel exosporium protein BetA used the finding of putative σK-directed promotor elements as a search criterium when looking for filipin genes encoding exosporium proteins in B. anthracis (Thompson et al., 2011a, b). Also exosporium proteins BclA and BxpA are preceded by a consensus sequence for a promotor recognized by σK (Sylvestre et al., 2002; Steichen et al., 2003). Unfortunately, we do not yet know the function of BC1245 as a bcΔ1245 mutant was unaltered in spore heat resistance, hydrophobicity, germination and outgrowth capacity when compared with wild-type B. cereus. Further characterization of the mutant spore would be valuable, for example, visualization of the outer spore surface by different microscopic techniques such as electron cryomicroscopy or atomic force microscopy as described by Kailas et al. (2011).

enterica (Grassl & Finlay, 2008; Haraga et al., 2008;

Tsolis et al., 2008; McGhie et al., 2009). This review presents a comparative analysis of the major genetic differences between S. Typhimurium and S. Typhi and how this may contribute Selleck AZD6244 to our understanding of typhoid pathogenesis. Organization of genomes allows us to gain a better understanding of the mechanisms by which species or serovars have evolved. Analysis of the chromosomal gene arrangement revealed that the genomic backbone of S. Typhimurium is very similar to the Escherichia coli genome. However, major differences in gene order have been observed in the S. Typhi chromosome. Differences in the S. Typhi genome occur mainly because of genomic rearrangements involving recombination between different rRNA operons (Liu & Sanderson, 1995; Liu & Sanderson, 1996) or IS200 elements (Alokam et al., 2002). Each serovar evolves through the acquisition of genetic elements by horizontal gene transfer or by gene degradation. The genomes of S. Typhimurium strain LT2 and S. Typhi strain CT18 are composed of 4 857 432 and 4 809 037 bp, respectively (Fig. 2) (McClelland et al., 2001; Parkhill et al., 2001). Both serovars share about 89% of genes (McClelland et al., 2001). Differences between

S. Typhimurium and S. Typhi include ≈480 genes unique to S. Typhimurium and ≈600 genes unique to S. Typhi (Parkhill et al., 2001). Salmonella pathogenicity islands (SPIs), plasmids, functional

prophages and phage remnants contribute significantly to the genetic diversity among S. enterica strains (Rotger Obatoclax Mesylate (GX15-070) & Casadesús, 1999; Boyd & Brüssow, 2002) and will be discussed below. The low level of genetic BMS 354825 variation observed in S. Typhi genomes of distinct isolates from around the world revealed a highly conserved and clonal relation, suggesting that they emerged from a single progenitor, making S. Typhi a monomorphic organism (Baker & Dougan, 2007; Holt et al., 2008). Clonality is often encountered in human-restricted pathogens (Achtman, 2008). There is very little evidence of adaptive selection in S. Typhi genes, with the exception of a recent evolution in phenotypic traits that includes the acquisition of resistance to fluoroquinolones (Chau et al., 2007; Le et al., 2007). Examination of DNA sequences and the rate of change of single-nucleotide polymorphisms suggest that S. Typhi may be only 50 000 years old, a short time frame for bacteria to accumulate diversity (Selander et al., 1990; Kidgell et al., 2002a, b; Roumagnac et al., 2006). This situation strongly suggests that evolution in the S. Typhi strain population is mainly characterized by loss of gene function. Salmonella enterica serovar Typhi is an example of reductive evolution, where the adaptation to its human niche has led to the functional inactivation of genes, due to certain needs that have been satisfied by the host (Dagan et al., 2006). Annotation of the first completed S.

This work was supported by FEDER and Fundação para a Ciência e a Tecnologia (FCT), Portugal (grants: PTDC/QUI/67925/2006, PTDC/BIA-MIC/71453/2006 and PTDC/EBB-BIO/100326/2008) and PhD fellowships to D.M.-H. and N.B. We thank Dr Raquel Seruca from IPATIMUP, University of Porto, Portugal, for her valuable contribution to the present work. We acknowledge Prof. Gerd Döring from University of INCB024360 clinical trial Tübingen

in Germany, Prof. John LiPuma from University of Michigan in USA and Prof. David Speert from University of British Columbia in Canada, who kindly provided Burkholderia strains. “
“A new strain of Beauveria bassiana was identified on the basis of the 18S rRNA gene sequence homology. This strain, called P2, is a spontaneously arisen mutant that was isolated after successive sub-culturing the wild-type B. bassiana P1 strain. P2 showed hyper-production of extracellular protease(s) as much as ninefold more than P1. An extracellular protease (SBP) having a molecular weight of 32 kDa was purified from the P2 strain. SBP was completely inhibited by the phenyl Romidepsin molecular weight methyl sulphonyl fluoride, which suggests that it belongs to the serine

protease family. Based on the homology analysis of its N-terminal and the gene sequences, the enzyme was identified as subtilisin. The enzyme displays maximum activity at 60 °C and pH 8, and was stable at pH 6–12. The enzyme hydrolyses natural proteins such as keratin and is activated in presence of β-mercaptoethanol and Tween detergents. SBP was compatible with some laundry detergent formulations and showed high efficacy in the removal of blood stains from cotton fabric. Moreover, it was observed to degrade the melanised feathers and to

hydrolyse the gelatine from X-ray films. Bay 11-7085 All these results highlight the suitability of SBP protease as a very efficient microbial bio-resource. “
“Stress-response sigma factor σH is negatively regulated by its cognate anti-sigma factor RshA in Streptomyces griseus. As the overexpression of RshA in the wild-type strain confers a distinctive bald phenotype (deficiency in aerial mycelium formation and streptomycin production), RshA is supposed to associate with not only σH but also another regulatory element that plays a crucial role in the developmental control of S. griseus. Here, we show that an anti-sigma factor antagonist BldG associates with RshA and negatively regulates its activity. The bald phenotype conferred by the overexpression of rshA was restored to the wild-type phenotype by the coexpression with bldG. The in vivo and in vitro protein interaction analyses demonstrated the specific association between RshA and BldG. A bldG mutant exhibited a distinctive bald phenotype and was defective in the σH-dependent transcription activities.

H. Chen, Chie-Pein Chen, Huey-Yi Chen, Jason Chen, Q. Chen, Zhengjun Chen, Zi-Jiang Cheng, Shi-Yann Cheng, Wenjun Chervenak, F. Chiba, Yoshihide Chigusa, Yoshitsugu Chisaka, Hiroshi Chiyoda, Tatsuyuki Chohan, Lubna Choi, Young-Min Chong, S. Chourmouzi, Danai Chung, Jacqueline P. W. Ciantar, E. Ciarmela, P. Cobellis, Luigi Codner, Ethel Coley, Sue Cristina, Rossi

Cuckle, H. Daher, Silvia Dane, Banu Dane, Cem Daniels, J. Danışman, Leyla Davila, G. Willy de Jong, P. de Laat, Monique Deans, Rebecca Deen, Suha Deffieux, Xavier Deligeoroglou, Efthimios Delotte, Jerome Dessole, S. Di Grezia, G. Dieter, Alexis A. Dik, Pieter Ding, Dah-Ching Dittrich, Ralf Dmitrieva, N. Dobashi, Kazuyoshi Dossus, Laure Douchi, Tsutomu Driák, Daniel Drosdzol-Cop, Agnieszka Du, Qiang Ducloy-Bouthors, A. S. Dundar, O. Dursun, Polat Dusse, Luci East, Christine Ebina, Yashuhiko Eblen, Scott Eguchi, Kazuo Ekambaram, Padmini El Saman, A. M. El-Shalakany, check details A. H. Enakpene, Christopher Ernest HY Ng, Ernest Ertas, Ibrahim Eshima, Nobuoki Eskandar, Osama Facchinetti, Fabio Fadare, O. Farghaly, Samir Fauconnier, Arnaud Fedorcsak, Peter Fenton, Tanis Ferrara, A. Ferrero, S. Fett, J. D. Fineschi, V. Fisher, Jane Fleisher, Jonah Florio, Tullio Fong, Alex Forbes, S. Fotopoulou, C. Fox, Nathan Franceschini, N. Francica, Giampiero Fritel, Xavier Fruscalzo,

Arrigo Fujii, Takuma Fujii, Tomoyuki Fujimori, Keiya Fujimoto, Akihisa Fujishita, Akira Fujita, Tomoyuki Fujita, Yasuyuki Fujito, Atsuya Fujiwara, Hisaya Fujiwara, Toshihiro Fukui, Atsushi Fukunaga, AZD0530 purchase Masaharu Fukuoka, Hideoki Fukushima, Akimune Fukushima, Kotaro Furuhashi, Madoka Furukawa, Naoto Fylstra, D. Gaffney-Stomberg, Erin Gajjar, K. Galazios, Georgios Ganguly, Bani Garfield, Robert Gärtner, Roland Gateva, Antoaneta Geller, Elizabeth J. Gershenson, David M. Ghezzi, Fabio Ghosh, Anuradha Giampietro, P. Giannella, Luca Gigue’re, aminophylline Yves Gilloteaux, Jacques Gimenez, Pepita Giulini, S. Giuntoli, R. L. 2nd Glavin, Kari Gleicher, Norbert Godfrey,

E. M. Goldfarb, H. A. Goldstein, Bram H. Goldstein, Steven R. Goncalves, Vania Gonzalez-Pinto, I. Goodman, M. P. Goodwin, Scott Goto, Aya Gourgiotis, Stavros Goya, Maria Goynumer, Gokhan Graham, Ernest Gray, J. Grisaru-Granovsky, S. Gultekin, Murat Güngör, Tayfun Güngördük, kemal Gupta, Nupur Guven, Suleyman Guvendag Guven, Emine Seda Haas, Brian J. Hachisuga, Toru Halder, Sunil Hale, Christopher Stephen Halhali, A. Haliloglu, Berna Hamada, Hiromi Hamano, Shinjiro Hanley, Krisztina Hanprasertpong, Jitti Hansen, Keith Haque, Khalid Hara, Toshimi Harada, Masafumi Harada, Miyuki Harada, Oi Harada, Tasuku Harada, Tatsuya Haruta, Shoji Hasegawa, Junichi Hasegawa, Kiyoshi Hashimoto, Kazunori Hashimoto, Shu Hata, Kenichiro Hata, Kohkichi Hata, Toshiyuki Hayakawa, Hiromi Hayakawa, Satoshi Hayata, Eijiro Heatley, Mark K. Heinonen, Pentti Henry, A. Heubner, Martin Heude, Barbara Hibino, Toshihiko Hickman, Nicola Hidaka, Nobuhiro Higuchi, Tsuyoshi Hill, J. B.

“
“In areas with low caries prevalence, indices are needed for caries detection, which can also be used to identify initial lesions. The aim of this study was to assess the caries prevalence among 12-year-olds using ICDAS criteria and to investigate the influence of independent variables on the findings. The study was conducted in two regions of Germany. In Region 1, children Selleck DAPT received regular school-based prophylaxis, including fluoride varnish 2×/yr. In Region 2, there was no use of fluoride varnish in schools. Information on different factors influencing the outcome variable of caries experience was collected using structured questionnaires.

DF-S values were calculated at different ICDAS cut-off points. To compare the mean caries scores of the subgroups, nonparametric

tests were performed. Variables associated with caries were included in a binary logistic regression analysis. At D1–6FS and D1+2FS level, the differences between the regions were statistically significant (P = 0.005 and P = 0.01, respectively). Regression analysis identified the variables ‘use of fluoridated toothpaste’, ‘fissure sealants’, and ‘ethnic origin’ as factors significant to the prevention of caries at various stages. In a population with low caries prevalence, significant differences between subgroups could only be found when initial lesions were included. “
“To compare the time-dependent changes in oral hygiene and periodontal health after restoring selleck compound primary posterior molars with a traditional stainless steel crown (SSC) or an aesthetic crown using various measures of periodontal health and oral hygiene. This investigation was a randomized, non-blinded prospective www.selleck.co.jp/products/AG-014699.html controlled clinical trial in which 264 crowns of different types were fitted onto the first and/or second primary molars of 76 children. The oral hygiene and the gingival health of the restored teeth and the antagonistic teeth were evaluated clinically and radiographically at 3- and 6-month intervals for 18 months after fitting the crowns. The periodontal health of

the control teeth was better than that of the remaining 215 restored teeth. The oral hygiene, as measured by the simplified oral hygiene index, and gingival health, as measured by the gingival index and the volume of gingival crevicular fluid, of the restored teeth, irrespective of crown type, progressively increased during the 18-month study period. Oral hygiene and gingival health around a restored primary tooth deteriorate with time. Our results suggest that SSC, an open-faced SSC, or a NuSmile® pediatric crown should be the preferred crown type for restoring posterior primary teeth. “
“International Journal of Paediatric Dentistry 2012; 22: 139–145 Objective.  For paediatric dentists, an indicator to assess caries risk of infants is very important.

Furthermore, these plasmids often undergo after transfer between different

sphingomonads pronounced rearrangements (Feng et al., 1997a, b; Ogram et al., 2000; Basta et al., 2004, 2005). Therefore, it seems that the maintenance, transfer and recombination of these plasmids are of major Cobimetinib cost importance for the exceptional degradative capabilities of this group of bacteria. The genomes of several sphingomonads have recently been sequenced, and therefore, also an increasing number of plasmid sequences from sphingomonads became available. It was therefore attempted to analyse the available plasmid sequence data in order to collect the currently accessible information about (degradative) plasmids in sphingomonads. The first example of a find more sequenced and carefully analysed degradative plasmid from a sphingomonad was plasmid pNL1 from Sphingomonas (now Novosphingobium) aromaticivorans F199, which carries all genes required for the degradation of biphenyl, naphthalene, m-xylene and p-cresol (Romine et al., 1999). Subsequently, the sequence analysis of plasmids pCAR3 (carrying all the genes for the mineralization of carbazole), pCHQ1 (coding for the linRED genes participating

in the degradation of γ-hexachlorocyclohexane) and pPDL2 (coding for a parathion hydrolase involved in organophosphate degradation) has been published (Shintani et al., 2007; Nagata et al., 2011; Pandeeti et al., 2012; Table 1). 86 362–87 666 YP_001165688.1 433 aa 84 603–85 808 YP_001165687.1 401 aa 83 388–84 371 YP_001165686.1 326 aa 209 439–210 644 YP_001165975.1

401 aa 212 040–213 242 YP_001165977.1 400 aa 210 877–211 962 either YP_001165976.1 361 aa 200 594–201 594 YP_718153.1 433 aa 202 396–203 658 YP_718154.1 420 aa 203 777–204 757 YP_718155.1 326 aa 1–1360 YP_003546976.1 387 aa 1360–2562 YP_003546977.1 400 aa 2607–3623 YP_003546978.1 338 aa 1–1104 YP_003543403.1 367 aa 1417–2052 YP_003543405.1 211 aa 1–654 YP_003550320.1 217 aa 19 777–20 880 YP_006965786.1 367 aa 21 193–21 828 YP_006965788.1 211 aa 84 694–85 854 EHJ57984.1 386 aa 86 021–87 223 EHJ57985.1 400 aa 87 506–88 327 EHJ57986.1 273 aa 2557–3339 WP_006949648 260 aa 43 879–44 637 WP_004213275 252 aa 42 857–43 882 WP_004213274 341 aa 51 3635–51 4939 CCA90427 434 aa 51 5490–51 6695 CCA90428 401 aa 51 6867–51 7844 CCA90429 325 aa 88 922–90 199 CCA89897 425 aa 86 441–87 634 CCA89895 397 aa 87 744–88 817 CCA89896 357 aa 45 176–45 961 CCA89804 261 aa 4081–5244 YP_007592251.1 376 aa 5439–6641 YP_007592252.1 400 aa 6686–7702 YP_007592253.1 338 aa 114 750–115 880 YP_007618239.1 376 aa 117 028–118 224 YP_007618241.1 398 aa 115 961–117 031 YP_007618240.1 356 aa 1–1104 YP_007592499.1 367 aa 1417–2052 YP_007592501 211 aa 37 217–38 329 AGH52044 370  aa 38 704–39 357 AGH52046 217 aa 101–1012 AGH52053.1 303 aa 1376–2011 AGH52055.1 211 aa 17 4080–17 5195 ABQ71384.1 371 aa 4708–5361 ABQ71231.1 217 aa 15 1005–15 3194 ABQ71370.1 729 aa 63 589–64 893 ABQ71573.1 434 aa 61 838–62 989 ABQ71572.1 383 aa 60 612–61 586 ABQ71571.1 324 aa 1–1164 YP_004831121.