First, the LSPR λ max of bare Au nanoshells was measured to be 830 nm. The LSPR λ max after incubation to the BSA solution

was measured to be 885 nm, corresponding to an additional 55-nm red shift, which was a wavelength shift two times larger than that of the reported nanohole substrate as a femtomole-level LSPR sensor [18]. Also, we confirmed that this peak position was not shifted after immersion in water. Furthermore, since the BSA molecule has no selective adsorption, this peak shift was attributed to the LSPR response to the changing of the local refractive index with the adsorption of BSA, which physically adsorbed to the gold surface of nanoshells and the substrate at the gap of nanoshells. It is indicated that we can improve the detection Temozolomide ic50 efficiency by localizing learn more the adsorption area of the target molecule without gold film directly laminated on the glass substrate. After immersion in water for 24 h, it is found that the λ max of nanoshell arrays returned to 834 nm. It is revealed that the

red shift of peak position was due to the physical adsorption of BSA proteins. Additionally, it is indicated that the LSPR peak did not return to its initial position because of the incomplete removal of BSA only with immersion in water. For application to bio/chemical detection devices, it should be noted that the signal transduction Chorioepithelioma mechanism in this nanosensor is a reliably measured wavelength shift in the NIR region. Figure 4 LSPR spectra of nanoshells before/after BSA attachment in (a) Au and (b) Cu nanoshell arrays. All spectra were collected in the air. Figure 4b shows the change

of LSPR properties taken from Cu nanoshell arrays before/after incubation to the BSA solution. In the air, the LSPR λ max of the bare Cu nanoshell arrays was measured to be 914 nm. Exposure to the BSA solution resulted in LSPR λ max = 944 nm, corresponding to an additional 30-nm red shift. In the case of Cu nanoshells, they exhibited a not so low sensitivity to the adsorption of molecule relative to Au. While Cu nanoshell arrays have problems to solve about their oxide layer and chemical stability, it is possible for inexpensive Cu to substitute for Au because of its sensitivity to the adsorption of biomolecule. We could evaluate the difference in LSPR sensing performance by changing the metal materials in the experiment. Conclusion In summary, we successfully fabricated uniform metal nanoshell arrays in a large area (30 × 60 mm2) on glass substrates and characterized the geometry and the optical properties based on the LSPR of the Au, Ag, and Cu nanoshell arrays. The LSPR λ max of Au and Cu were at longer wavelengths than that of Ag nanoshell arrays of similar structural parameters. This result indicates that Au and Cu are superior to Ag as materials for NIR light-responsive plasmonic sensors.

The presented synthetic strategy allows a good control of NC size and distribution within the polymer matrix as required for the application in photovoltaic cells. Conclusions An in situ synthetic route for the realization of hybrid polymer/nanocomposite materials was presented. We demonstrated that the soluble metal thiolate derivative [Cd(SBz)2]2·MI, obtained using 1-methylimidazole as cadmium ligand, is a suitable starting material

to grow CdS NCs in semiconducting polymeric matrices. We found that the precursor decomposition and the subsequent NCs nucleation and growth start at temperatures below 200°C, namely already at 175°C and in relatively short time (30min), the temperature lowering being crucial for avoiding possible damage or deterioration of the matrix. Such a result allows extending the range of suitable matrices to thermally soft polymers such as MEH-PPV towards the fabrication of organic–inorganic nanocomposite materials Pirfenidone for optoelectronics and light harvesting. The structure of [Cd(SBz)2]2·MI also helps in obtaining a homogeneous

spatial dispersion of the molecule itself inside the polymer promoting the formation of a highly uniform network and well-dispersed NCs. The weight ratio of the precursor to the polymer directly determines the number density of the NCs as well as the coverage uniformity, the optimal value being 2:3. The synthetic route this website did not significantly alter the polymer resistance to deformation, further demonstrating the applicability in the field of large-area, flexible, low-cost solar cells production via spinning or soft moulding lithography. Acknowledgements This work was supported by the Regione Puglia (Bari, Italy) – Project PONAMAT (PS_016). References 1. Wang D: Semiconductor nanocrystal-polymer composites: using polymers for nanocrystal processing. In Semiconductor nanocrystal quantum dots. Edited by: Rogach AL. New

York: Springer; 2008:170–196. 2. Neves AAR, Nintedanib (BIBF 1120) Camposeo A, Cingolani R, Pisignano D: Interaction scheme and temperature behavior of energy transfer in light-emitting inorganic–organic composite system. Adv Funct Mater 2008, 18:751–757.CrossRef 3. Tamborra M, Striccoli M, Comparelli R, Curri ML, Petrella A, Agostiano A: Optical properties of hybrid composites based on highly luminescent CdS nanocrystals in polymer. Nanotechnology 2004, 15:S240-S244.CrossRef 4. Garcia M, van Vliet G, Jain S, Schrauwen BAG, Sarkissov A, van Zyl WE, Boukamp B: Polypropylene/SiO 2 nanocomposites with improved mechanical properties. Rev Adv Mater Sci 2004, 6:169–175. 5. Novak BM: Hybrid nanocomposite materials between inorganic glasses and organic polymer. Adv Mater 1993, 5:422–433.CrossRef 6. Colvin VL, Schlamp MC, Alivisatos AP: Light-emitting diodes made from cadmium selenide nanocrystals and a semiconducting polymer. Nature 1994, 370:354–357.CrossRef 7.

0. Hydrogenase activity-staining was done as described in [18] with 0.5 mM benzyl viologen (BV) and 1 mM 2,3,5,-triphenyltetrazolium

chloride (TTC) and continuous flushing with highly pure hydrogen gas until the activity bands appeared except that the buffer used was 50 mM MOPS pH 7.0. Alternatively, staining was done in hydrogen-flushed buffer using 0.3 mM phenazine methosulfate (PMS) as mediator and 0.2 mM nitroblue tetrazolium (NBT) as electron acceptor [52]. When formate was added as substrate to the buffer, a final concentration of 50 mM was used. When used in native-PAGE molecular mass standard proteins from a gel filtration markers kit 29-700 kDa (Sigma) were mixed in equal amounts and 6 μg of each were loaded on the gel. Immunological and enzymic methods Western blotting was performed as described in [53] by transferring proteins to nitrocellulose membranes and challenging them with monoclonal penta-His antibody from mouse (Qiagen) or Y-27632 solubility dmso polyclonal anti-Hyd-1 antibody (1:20000). Secondary goat-anti-mouse or anti-rabbit antibody, respectively conjugated with HRP enzyme (Bio-Rad, USA) was used for visualisation with the Immobilon Western chemiluminescent HRP substrate (Millipore, USA). Purification

of active Hyd-1 from a 5 L culture of strain FTH004 (His-HyaA) grown in TGYEP, Crizotinib price pH 6.5 supplemented with 5 μM Ni2+ was carried out as described [34]. Determination of protein concentration was done by the method of Bradford (Bio-Rad, USA) [54]. Measurement of redox potential Aliquots of 50 mM MOPS buffer pH 7.0 containing the concentrations of the respective Amino acid redox dyes indicated above were either incubated overnight in an anaerobic chamber with

an atmosphere containing 5% hydrogen for 6 h or was bubbled with hydrogen gas (100% atmosphere) for 30 min and the redox potential determined using a EMC 30-K010-D redox micro-electrode (Sensortechnik Meinsburg GmbH, Germany) attached to a Lab850 pH/redox meter (Schott Instruments, Germany). The electrode was standardized using a redox buffer provided by the company. Measurements were performed two times. Acknowledgements We are grateful to Alison Parkin for providing the oxygen-sensitive hydrogenase 1 strains and to Stefanie Hartwig for help with the redox potential measurements. Martin Sauter is thanked for providing strain HDK101. This work was supported by the BBSRC grant BB/I02008X/1 to FS and DFG grant SA 494/3-1 to RGS. References 1. Forzi L, Sawers RG: Maturation of [NiFe]-hydrogenases in Escherichia coli. Biometals 2007, 20:565–578.PubMedCrossRef 2. Böck A, King P, Blokesch M, Posewitz M: Maturation of hydrogenases. Adv Microb Physiol 2006, 51:1–71.PubMedCrossRef 3. Menon NK, Robbins J, Wendt J, Shanmugam K, Przybyla A: Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1. J Bacteriol 1991, 173:4851–4861.PubMed 4.

In a recent review, Kobayashi et al. [36] discussed the enhancement of radiobiological effects by heavy elements, in particular gold and platinum. Auger enhancing phenomena to electron and Hadron therapy is also suggested which broadens furthermore their therapeutic applications. In another study [37] we have used Proteases inhibitor the same chemotherapy protocol, but a different irradiation scheme: the dose was delivered

in three fractions of 5 Gy using 6 MV photons and the whole brain was irradiated, beginning on the day after drug administration, using the same Alzet osmotic pumps. The results are very consis-tent with the data presented here, the chemotherapy groups had the comparable survival rates (MST of 77 d ± 23.0 and 71 d ± 7 and 16%, 14% long term survival rates, respectively). PF-562271 Rats bearing tumors, treated with carboplatin and X-irradiation had MST and (MeST) of 111.8 d (78 d), with 40% surviving more than 180 d (i.e.

cured), compared to 77.2 d (59 d) for pump delivery of carboplatin alone and 31.8 d (32 d) for X-irradiated alone. There was no microscopic evidence of residual tumor in the brains of all long-term survivors. The biologically equivalent dose-fraction (BED) can be calculated using the classic linear quadratic equation [38, 39]: (1) where n is the number of fractions, d is the dose per fraction in Gy, and α and β are two variables that indicate the sensitivity of tumor or normal tissue to changes in dose fractionation. The α/β ratio is usually taken to be 10 for tumor and early-reacting tissues and 3 for late-reacting tissues like brain. The biologically effective dose (BED) for 15 Gy, delivered in a single fraction, using the α/β ratios indicated above, is

37.5 Gy in Atorvastatin acute and tumor effects and 90 Gy in late effects (37). In comparison, the BEDs for 15 Gy delivered in three fractions of 5 Gy each are largely lower: 22.5 and 40.0 Gy, for tumor and normal brain, respectively. The dose per fraction should be 8 Gy, for obtaining BEDs in a three fractions regimen equivalent to those of 15 Gy delivered in a single fraction [11]. The enhanced survival results obtained using a single fraction of 15 Gy, using either 6 MV X-rays (this study) or synchrotron radiation [12], in comparison with 15 Gy delivered in 3 fractions [37] is in good agreement with the calculated equivalent BEDS of these irradiation schemes. Conclusions The present study firmly establishes the equivalency of i.c. administration of carboplatin either by infusion via osmotic pumps or CED with irradiation with 6 MV X-rays and synchrotron X-rays. Since medical LINACs are widely available worldwide, this could provide the opportunity to clinically evaluate this combination therapy at multiple centers.

2D). In cluster D the dctA gene coding for the DctA dicarboxylate import system was found. The DctA dicarboxylate import system [37] is well characterised and a broad substrate range has been identified [38]. This dicarboxylate import system is known to be essential for symbiosis since it is supposed to Target Selective Inhibitor Library provide the cells in the bacteroid state with tricarbonic acid (TCA) cycle intermediates from the host plant, e.g. succinate, malate, and

fumarate. A group of genes in this cluster points to an induced fatty acid degradation. The gene smc00976 is coding for a putative enoyl CoA hydratase and smc00977 and smc02229 are coding for putative acyl CoA dehydrogenase proteins. With glpD, a gene coding for a glycerol-3-phosphate dehydrogenase find more involved in the glycerol degradation could also be found in cluster D. The transient induction of genes involved in fatty acid degradation might be related to a lack of energy or the modification of the membrane lipid composition. Cluster E contains genes involved in nitrogen metabolism, ion transport and methionine metabolism Cluster E consists of 22 genes whose expression was lowered in response to the pH shift. The expression was lowered up to 10 minutes after pH shift and then stayed constant until the end of the time course experiment (Fig. 2E). Cluster E contains genes involved in nitrogen metabolism.

The gene glnK codes for a PII Carnitine palmitoyltransferase II nitrogen regulatory protein activated under nitrogen limiting conditions and forms together with amtB, which encodes a high affinity ammonium transport system, an operon. The GlnK protein could also be identified as lower expressed after a short exposure of S. medicae cells to low pH [27].

It was argued by Reeve et al. that this observation might be related to some crosstalk between nitrogen and pH sensing systems during the early pH adaptation [27]. With metF, metK, bmt, and ahcY four genes involved in the methionine metabolism were also grouped in this cluster, while two other met genes were grouped into cluster F (metA) and cluster G (metH), respectively. The distribution of these genes to two other clusters of down-regulated genes might be due to the fact the met genes are not organised in an operon, but dispersed over the chromosome. S-adenosylmethionine is formed from methionine by MetK and is the major methylation compound of the cell that is needed e.g. for polyamine- or phosphatidylcholine biosynthesis. The connection between the down-regulation of the methionine metabolism and the pH response is not clear. It was shown that various abiotic stresses result in a rapid change of cellular polyamine levels [39–41]. Several genes belonging to ion uptake systems were located in cluster E, like the complete sitABCD operon and phoC and phoD of the phoCDET operon. The sitABCD operon codes for a manganese/iron transport system [42, 43].

In investigating the passivation effect of the a-Si:H shell, we find that the combination

of the a-Si:H shell and SiNW solar cell leads to enhanced power conversion efficiency, open-circuit voltage, and short-circuit current by more than selleck screening library 37%, 15%, and 12%, respectively, compared to the SiNW cells. This is mainly due to the suppression of the surface recombination of the large surface area of SiNWs. We expect that the a-Si:H will have a significant role in passivation of the SiNW surface with more optimization of its thickness and more theoretical understanding of its interface with SiNWs. Acknowledgements This work has been funded by the Ministry of Science, Technology and Innovation, Malaysia, and Solar Energy Research Institute (SERI), UKM. References 1. Huia S, Zhang J, Chena X, Xua H, Maa D, Liua Y, Taoa B: Study of an amperometric glucose sensor based on Pd–Ni/SiNW electrode. Sensor Actuator B Chem 2011, 155:592–597.CrossRef 2. Zaremba-Tymieniecki M, Li C, Fobelets K, Durrani ZAK: Field-effect transistors using

silicon nanowires prepared by electroless chemical etching. IEEE Electron Device Lett 2010, 31:860–862.CrossRef drug discovery 3. Huang Z, Zhang X, Reiche M, Liu L, Lee W, Shimizu T, Senz S, Gösele U: Extended arrays of vertically aligned sub-10 nm diameter [100] Si nanowires by metal-assisted chemical etching. Nano Lett 2011, 8:3046–3051.CrossRef 4. Jung JY, Guo Z, Jee SW, Um HD, Park KT, Hyun MS: A waferscale Si wire solar cell using radial and bulk p–n junctions. Nanotechnology 2010, 21:5303–5306. 5. Kumar D, Srivastava SK, Singh PK, Husain M, Kumar V: Fabrication of silicon Amisulpride nanowire arrays based solar cell with improved performance. Sol Energy Mater Sol Cells 2011, 95:215–218.CrossRef 6. Peng K, Xu Y, Wu Y, Yan Y, Lee ST, Zu J: Aligned single crystalline silicon nanowire arrays for photovoltaic applications. Small 2005, 1:1062–1067.CrossRef 7. Kodambaka S, Tersoff J, Reuter CM,

Ross MF: Diameter-independent kinetics in the vapor–liquid-solid growth of Si nanowires. Phys Rev Lett 2006, 96:6105–6108.CrossRef 8. Zhang YF, Tang YF, Wang N, Lee CS, Bello I, Lee ST: Silicon nanowires prepared by laser ablation at high temperature. Appl Phys Lett 1998, 72:1835–1837.CrossRef 9. Niu J, Sha J, Yang D: Silicon nanowires fabricated by thermal evaporation of silicon monoxide. Phys E 2004, 23:131–134.CrossRef 10. Holmes DJ, Johnston PK, Doty CR, Korgel AB: Control of thickness and orientation of solution-grown silicon nanowires. Science 2000, 287:1471–1473.CrossRef 11. Huang Z, Fang H, Zhu J: Fabrication of silicon nanowire arrays with controlled diameter, length, and density. J Adv Mater 2007, 19:744–19748.CrossRef 12. Dai AH, Chang CH, Lai YC, Lin AC, Chung JR, Lin RG, He HJ: Subwavelength Si nanowire arrays for self-cleaning antireflection coatings. J Mater Chem 2010, 20:10924–10930.CrossRef 13.

Acknowledgments This work is supported by the Important National Science & Technology Specific Projects (2011ZX02702-002), the National Natural Science Foundation of China (no. 51102048), SRFDP (no. 20110071120017), and the Independent Innovation Foundation of Fudan University, Shanghai. References 1. Lewis BG, Paine DC: Applications and processing of transparent conducting oxides. MRS Bull 2000, 25:2.CrossRef 2. Shah A, Torres P, Tscharner R, Wyrsch N, Keppner H: Photovoltaic technology: the case for thin-film solar cell. Science 1999, 285:692.CrossRef 3. Jagadish C, Pearton S: Zinc Oxide Bulk, Thin Films and Nanostructures. Oxford: Elsevier; 2006. 4. Shan FK, Liu GX, Lee WJ, Shin Galunisertib supplier BC:

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ZnO films. Opt Mater 2007, 29:1548.CrossRef 12. Lin SS, Huang JL, Sajgalik P: The properties of Ti-doped ZnO films deposited by simultaneous RF and DC magnetron sputtering. Surf Coat Technol 2005, 191:286.CrossRef 13. Roth AP, Williams DF: Properties of zinc oxide films prepared by the oxidation of diethyl zinc. J Appl Phys 1981, 52:6685.CrossRef 14. Khan OFZ, O’Brien P: On the use of zinc acetate as a novel precursor for the deposition of ZnO by low-pressure metal-organic chemical vapor deposition. Thin Solid Films 1989, 173:95.CrossRef 15. Sernelius BE, Berggren KF, Jin ZC, Hamberg I, Granqvist CG: Band-gap tailoring of ZnO by means of heavy Al doping. Phys Rev B 1998, 37:10244.CrossRef 16. Fons P, Yamada A, Iwata K, Matsubara K, Niki S, Nakahara K, Takasu H: An EXAFS and XANES study of MBE grown Cu-doped ZnO. Nucl Instrum Methods Phys Res B 2003, 199:190.CrossRef 17.

A, distribution of cells in G1 (blue),

S (red) and G2 (green) phases for batch cultures of PCC9511 grown under HL. B, same for HL+UV conditions. The experiment was done in duplicates shown by filled and Inhibitor Library empty symbols. Note that only the UV radiation curve is shown in graph B since the visible light curve is the same as in graph A. White and black bars indicate light and dark periods. The dashed line indicates the irradiance level (right axis). HL, high light; PAR, photosynthetically available radiation; UV, ultraviolet radiation. Figure 1 shows the time course variations of the percentages of cells in the different phases of the cell cycle. Under HL condition, cells started to enter the S phase about 4 h before the light-to-dark transition (LDT) and the peak of S cells was reached exactly at the LDT. The first G2 cells appeared at the LDT and the peak of G2 cells was reached 4 h later. Most cells had completed division before virtual sunrise, as shown by a percentage of cells in learn more G1 close to 100% at (or 1 h after) that time (Fig. 1A). PCC9511 cultures acclimated to HL+UV conditions showed a remarkable cytological response with

regard to the timing of chromosome replication. In the presence of UV, entry into S was clearly delayed, with the onset of chromosome replication occurring about 1 h before the LDT and the maximum number of cells in S phase reached 2 h after the LDT. Entry into G2 was also delayed by 3 h, but the peak of G2 cells was reached more quickly, so that it occurred on average only 1 h after that observed under the HL condition (Fig. 1B). The faster progression of cells through S and G2 phases under HL+UV than HL only conditions in batch culture was confirmed by calculating the lengths of the S and Exoribonuclease G2 phases, which were shorter

in the former condition (Table 1). Cells grown under HL+UV exhibited a higher level of synchronization (as shown by a lower synchronization index, Sr) than those grown under HL only. However, the calculated growth rates were not significantly different between the two conditions. Therefore, the dose of UV irradiation that was used in this experiment did not prevent cells from growing at near maximal rate despite the delay of entry in S phase (Table 1). It must be noted that growth rates calculated from the percentages of cells in S and G2 (μcc) using the method described by Carpenter & Chang [30] were systematically about 10% higher than those calculated from the change in cell number (μnb). Since the latter method was used to assess the growth rate of continuous cultures (see below), these experiments in batch cultures were therefore useful to estimate the bias brought by these cell cycle-based growth rate measurements.

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C, Wharam P, Weschler L: Three independent biological mechanisms cause exercise-associated hyponatremia: evidence from 2,135 weighed competitive athletic performances. Proc Natl Acad Sci USA 2005, 102:18550–18555.PubMedCrossRef 21. Irving RA, Noakes TD, Buck R, van Zyl Smit R, Raine E, Godlonton J, Norman RJ: Evaluation BMS-777607 nmr of renal function and fluid homeostasis during recovery from exercise-induced hyponatremia. J Appl Physiol 1991, 70:342–348.PubMed 22. Sharwood K, Collins M, Goedecke J, Wilson G, Noakes T: Weight changes, sodium levels, and performance in the South African Ironman Triathlon. Clin J Sport Med 2002, 12:391–399.PubMedCrossRef 23. Speedy DB, Noakes Paclitaxel mw TD, Kimber NE, Rogers IR, Thompson JM, Boswell DR, Ross JJ, Campbell RG, Gallagher PG, Kuttner JA: Fluid balance during and after an ironman triathlon. Clin J Sport Med 2001, 11:44–50.PubMedCrossRef 24. Noakes TD: Changes in body mass alone explain almost

all of the variance in the serum sodium concentrations during prolonged exercise. Has commercial influence impeded scientific endeavour? Br J Sports Med 2011, 45:475–477.PubMedCrossRef 25. Sharwood KA, Collins M, Goedecke JH, Wilson G, Noakes TD: Weight changes, these medical complications, and performance during an Ironman triathlon. Br J Sports Med 2004, 38:718–724.PubMedCrossRef 26. Chorley J, Cianca J, Divine J: Risk factors for exercise-associated hyponatremia in non-elite marathon runners.

Clin J Sport Med 2007, 17:471–477.PubMedCrossRef 27. Rosner MH, Kirven J: Exercise-associated hyponatremia. Clin J Am Soc Nephrol 2007, 2:151–161.PubMedCrossRef 28. Lehmann M, Huonker M, Dimeo F, Heinz N, Gastmann U, Treis N, Steinacker JM, Keul J, Kajewski R, Häussinger D: Serum amino acid concentrations in nine athletes before and after the 1993 Colmar ultra triathlon. Int J Sports Med 1995, 16:155–159.PubMedCrossRef 29. Mischler I, Boirie Y, Gachon P, Pialoux V, Mounier R, Rousset P, Coudert J, Fellmann N: Human albumin synthesis is increased by an ultra-endurance trial. Med Sci Sports Exerc 2003, 35:75–81.PubMedCrossRef 30. Maughan RJ, Whiting PH, Davidson RJ: Estimation of plasma volume changes during marathon running. Brit J Sports Med 1985, 19:138–141.CrossRef 31. Hew-Butler T, Jordaan E, Stuempfle KJ, Speedy DB, Siegel AJ, Noakes TD, Soldin SJ, Verbalis JG: Osmotic and nonosmotic regulation of arginine vasopressin during prolonged endurance exercise. J Clin Endocrinol Metab 2008, 93:2072–2078.PubMedCrossRef 32.

The list of the isolates, their serological and VNTR-based identifications are presented in Table 1. Table 1 New Caledonian Leptospira isolates analyzed in the present study. Isolate Species Serogroup VNTR-based serovar [13] Source 1989-01 L. interrogans Icterohaemorragiae Copenhageni or Icterohaemorragiae human 1995-06 L. interrogans Icterohaemorragiae Erlotinib Copenhageni or Icterohaemorragiae human 1989-07 L. interrogans Icterohaemorragiae Copenhageni or Icterohaemorragiae human 1995-09 L. interrogans Icterohaemorragiae Copenhageni or Icterohaemorragiae human 2000-14 L. interrogans Icterohaemorragiae

Copenhageni or Icterohaemorragiae human 1995-01 L. interrogans Pomona Pomona human 1989-03 L. interrogans Pomona Pomona human 1997-05 L. interrogans Pomona Pomona human 1990-17 L. interrogans Pomona Pomona human LTDV15 L. interrogans Pomona Pomona deer (1992) 1993-01 L. interrogans Pyrogenes

unidentified human 1993-04 L. interrogans Pyrogenes unidentified human 1995-04 L. interrogans Pyrogenes unidentified human 1999-07 L. interrogans Pyrogenes unidentified human 1989-08 L. interrogans Pyrogenes unidentified human 1995-03 L. borgpetersenii Ballum Castellonis human 1999-12 L. borgpetersenii Ballum Castellonis human 1990-13 L. borgpetersenii Ballum Castellonis human 1990-14 L. borgpetersenii Ballum Castellonis human LTDV14 L. borgpetersenii Sejroe Hardjo (type Hardjo-bovis) deer (1992) GenBank accession numbers selleck compound www.selleck.co.jp/products/atezolizumab.html of the sequences obtained from these isolates are provided as additional file 1 Table S1. Clinical specimens Clinical samples (sera) routinely received at Institut Pasteur in Nouméa, for the diagnosis of leptospirosis were also

included in the study. We studied 88 human PCR positive sera collected from January 2008 to February 2010. Twelve PCR-positive deer kidney samples collected in 2010 during a sampling campaign in a slaughterhouse were also included. The 27 human samples used for drawing phylogenic trees are summarized in Table 2. Table 2 Clinical specimens analyzed in the present study. Specimen identification Source Leptospira concentration based on qPCR [15] lfb1-based cluster (see results) 08323250 Human serum < 50/ml L. borgpetersenii 1 08238362 Human serum < 50/ml L. interrogans 3 09022251 Human serum < 50/ml L. interrogans 2 09037333 Human serum < 50/ml L. interrogans 3 09046172 Human serum < 50/ml L. interrogans 2 09068284 Human serum < 50/ml L. borgpetersenii 1 09106497 Human serum < 50/ml L. interrogans 2 09110512 Human serum < 50/ml L. interrogans 4 09139265 Human serum < 50/ml L. borgpetersenii 1 09162317 Human serum < 50/ml L. borgpetersenii 1 09337238 Human serum < 50/ml L. interrogans 3 10032221 Human serum < 50/ml L. borgpetersenii 1 10073167 Human serum < 50/ml L. interrogans 1 08099430 Human serum (fatal case) 50/ml L.