J Appl Physiol 2004, 97:39–44 PubMedCrossRef 25 Coris EE, Ramire

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AM, Van Durme DJ: Heat illness in athletes: the dangerous combination of heat, humidity and exercise. Sports Med 2004, 34:9–16.PubMedCrossRef 26. Evans GH, Shirreffs SM, Maughan RJ: Postexercise rehydration in man: the effects of carbohydrate content and osmolality of drinks ingested ad libitum. Appl Physiol Nutr Metab 2009, 34:785–793.PubMedCrossRef ICG-001 order 27. Casa DJ, Armstrong LE, Hillman SK, Montain SJ, Reiff RV, Rich BS, Roberts WO, Stone JA: National Athletic Trainers’ Association Position Statement: Fluid Replacement for Athletes. J Athl Train 2000, 35:212–224.PubMed 28. Convertino VA, Armstrong LE, Coyle EF, Mack GW, Sawka MN, Senay LC Jr, Sherman WM: American College of Sports Medicine position stand. Exercise and fluid replacement. Med Sci Sports Exerc 1996, 28:i-vii.PubMed 29. Bouchama A, Knochel JP: Heat stroke. N Engl J Med 2002, 346:1978–1988.PubMedCrossRef 30. van Nieuwenhoven MA, Vriens BE, Brummer RJ, Brouns F: Effect

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Controlled trial of methyl

Controlled trial of methylprednisolone pulses and low dose oral prednisone for the minimal change nephrotic syndrome. Br Med J (Clin Res Ed). 1985;291:1305–8.CrossRef 2. Faul C, Donnelly M, Merscher-Gomez S, Chang YH, Franz S, Delfgaauw J, et al. The actin cytoskeleton of kidney podocytes is a direct target of the antiproteinuric effect of cyclosporine A. Nat Med. 2008;14:931–8.PubMedCrossRef 3. Takei T, Koike M, Suzuki K, Shirota S, Itabashi M, Ohtsubo S, et al. The characteristics of relapse in adult-onset Stattic ic50 minimal-change nephrotic syndrome. Clin Exp Nephrol. 2007;11:214–7.PubMedCrossRef 4. Nakayama M, Katafuchi R, Yanase T, Ikeda

K, Tanaka H, Fujimi S. Steroid responsiveness and frequency of relapse in adult-onset minimal change nephrotic syndrome. Am J Kidney Dis. 2002;39:503–12.PubMedCrossRef 5. Yorgin PD, Krasher selleck chemical J, Al-Uzri AY. Pulse methylprednisolone treatment of idiopathic steroid-resistant nephrotic syndrome. Pediatr Nephrol. 2001;16:245–50.PubMedCrossRef 6. Fukudome K, Fujimoto S, Sato Y, Kitamura K. Comparison of the effects of intravenous methylprednisolone pulse versus oral prednisolone therapies on the first attack of minimal-change nephrotic syndrome in adults. Nephrology. 2012;17:263–8.PubMedCrossRef 7. Eguchi A, Takei T, Yoshida T, Tsuchiya K, Nitta K. Combined cyclosporine and prednisolone therapy in adult patients

with the first relapse of minimal-change nephrotic syndrome. Nephrol PRKACG Dial Transplant. 2010;25:124–9.PubMedCrossRef 8. Matsumoto H, Nakao T, Okada T, Nagaoka Y, Takeguchi F, Tomaru R, et al. Favorable outcome of low-dose cyclosporine after see more pulse methylprednisolone in Japanese adult minimal-change nephrotic syndrome. Intern Med. 2004;43:668–73.PubMedCrossRef 9. Hamasaki Y, Yoshikawa N, Hattori S, Sasaki S, Iijima K, Nakanishi K, et al. Cyclosporine and steroid therapy in children with steroid-resistant nephrotic syndrome. Pediatr Nephrol. 2009;24:2177–85.PubMedCrossRef 10. Radhakrishnan J, Cattran DC. The KDIGO practice guideline on glomerulonephritis: reading between the (guide)lines–application to the individual

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Some of these transcription factors are known to be involved in p

Some of these transcription factors are known to be involved in positive regulation of gene expression (LuxR, AraC). Others are involved in repression (DeoR, MerR), while members of IclR and LysR families could be activators or repressors of gene expression [22]. Nevertheless, the contribution of these regulators and

their targets to B. melitensis internalization epithelial cells has not been fully examined. The locus encoding the alternative sigma 32 factor (BMEI0280) that allows Brucella to survive under general stress situations was up-regulated in stationary phase cultures. The BMEI1789 locus that encodes a subunit of the other alternative sigma 54 factor (rpoN), which allows transcription of those genes involved in utilization Syk inhibitor of nitrogen and carbon sources and energy metabolism, was up-regulated in late-log phase cultures compared to stationary phase cultures. Two-component transcriptional regulators are comprised of a cytoplasmic membrane-located sensor protein and a cytoplasmic response regulator protein [23]. Eight ORFs encoding for two-component response regulators have been identified in the B. melitensis 16 M genome [19]. Selleck ABT888 One of the signal transduction-encoded genes up-regulated in late-log phase cultures (vsr; BMEI1606), was previously identified in B. melitensis attenuated mutants [24]. The other

(hprK; BMEI2034) is a central regulator of carbohydrate metabolism genes and also plays a role in virulence development of certain pathogens [25]. Although the molecular regulation Clomifene of these response regulators in B. melitensis is currently unknown, understanding how vsr, hprK and others are regulated, could offer insight into B. melitensis virulence. Identifying the target genes of these transcriptional regulators would significantly clarify the role of growth-phase in Brucella physiology, metabolism and virulence regulation. Almost all GSK2118436 research buy differentially expressed genes encoding cell envelope and outer membrane components were up-regulated in late-log phase cultures The ability of Brucella to invade cells has been linked to its outer membrane (OM) properties, as well as to structures built within

the cell envelope [26, 27]. Twenty-six genes directly involved in cell envelope and outer membrane biogenesis were differentially expressed at late-log compared to stationary phase of growth. These included genes that encode outer membrane proteins (BMEI0402, BMEI0786), lipoproteins (BMEI0991, BMEI1079), LPS (BMEI0418, BMEI0586, BMEI0833, BMEI1414), and peptidoglycan biosynthesis (BMEI0271, BMEI0576). The main COGs functional category of genes that were up-regulated in B. melitensis cultures at late-log compare to stationary phase of growth were ORFs encoding membrane transport proteins. These included genes encoding transporters specific for amino acids (BMEI0263–0264, BMEII0098–9 and BMEII0861 to II0864), carbohydrates (BMEI1580, BMEI1713, BMEII0621–2 and II0624) and uncharacterized transporters (BMEI1554, BMEII0481, BMEII0483, BMEII0662).

Western analyses of eIF2α phosphorylation in the strains expressi

Western analyses of eIF2α phosphorylation in the strains expressing zebrafish PKR and the various vIF2α mutants revealed that vIF2α, vIF2α+26C,

vIF2α59C led to strong and comparable inhibition of eIF2α phosphorylation (Figure 5D, next to bottom panel, selleck lanes 2-4). Consistent with their inability to inhibit PKR toxicity in yeast, high levels of eIF2α phosphorylation were observed in strains expressing the other vIF2α mutants (Figure 5D). As seen earlier, PKR was expressed at higher levels and migrated faster on SDS-PAGE when PKR toxicity and eIF2α phosphorylation were suppressed (Figure 5D, top panel). Western blot analyses using antibodies against a C-terminal Myc-epitope tag in the vIF2α constructs revealed detectable expression for only vIF2α, vIF2α+26C, and vIF2α59C. Comparable results were obtained in Western blot analyses of protein extracts from the control (-PKR) strain eFT-508 research buy expressing these same vIF2α mutants (data not shown), buy SC79 indicating that both the S1 domain and the helical domain are essential for vIF2α expression and/or stability. Figure 5 Both S1 and helical domains in vIF2α are required for PKR inhibition. (A) Schematic representation of RCV-Z vIF2α constructs tested in yeast growth assays and Western blots analyses. S1 domain (red), helical domain (HD;

blue) and C-terminal domain (CTD, yellow) are represented by boxes. Numbers that follow deltas (Δ) indicate the(number of residues that were deleted from the C- or N-terminus, respectively. The extended C-terminus (26 amino acids) from ATV vIF2α was added to the C-terminus of RCV-Z vIF2α in the constructs with the +26C label. The indicated constructs were introduced into isogenic yeast strains having either an empty vector (B, J673) or a GAL-CYC1-zebrafish PKR construct (C, J944) integrated at the LEU2 locus. The indicated transformants were streaked on SC-Gal medium where expression of both PKR and the viral

proteins was induced, and incubated at 30°C for 4 days. Results shown are representative of 4 independent transformants for each plasmid. (D) Transformants Fludarabine order described in panels B-C were grown in liquid SC-Gal medium for 13 hours, then whole cell extracts were obtained from equal numbers of cells and subjected to SDS-PAGE followed by immunoblot analysis. Following transfer to nitrocellulose membranes, the upper half of the blot was probed with anti-Flag tag antibodies, which detect Flag-tagged zebrafish PKR (top panel). The lower part of the blot was incubated with anti-Myc tag antibodies to detect Myc-tagged vIF2α (second panel from top), then stripped and probed with phosphospecific antibodies against Ser51 in eIF2α (eIF2α-P; third panel from top), and finally stripped again and probed with polyclonal antiserum against total yeast eIF2α (bottom panel).

In contrast to T47D cells, BC-ER cells grew slower

after

In contrast to T47D cells, BC-ER cells grew slower

after being treated with E2, and cell proportion in the G2 + S period was reduced. This result is consistent with previous studies showing that E2 inhibits the growth of ERα-positive breast cancer cells transformed from ERα-negative cells [29–31]. We supposed that drug resistance of BC-ER cells was due to its low growth velocity in the presence of E2. However, the apoptosis-regulating proteins Bcl-2 and Bax, which are considered as important proteins mediating drug resistance in ERα-positive breast cancer cells, may not play a role in the formation of drug resistance of BC-ER cells. The results obtained above showed that ERα activation increased the sensitivity of natural ERα-positive T47D breast cancer cells to different chemotherapeutic agents, and that the inhibition of MM-102 supplier ERα activation by fulvestrant resulted in chemoresistance. Meanwhile, ERα activation decreased Selleck Epacadostat the chemosensitivity of ERαCitarinostat nmr -stably transfected BC-ER cells. Compared with ERα-negative BC-V cells, ERα-positive BC-ER cells presented higher resistance to multiple chemotherapeutic agents. We could not explain these phenomena

by stating that ERα mediated the drug resistance of breast cancer cells to chemotherapy through the regulation of the expression of Bcl-2 and Bax. This is because ERα activation upregulated the expression of Bcl-2 in natural ERα-positive breast cancer cells, however, ERα activation downregulated Bcl-2 expression and upregulated Bax expression in ERα-positive cancer cells transformed the from ERα-negative breast cancer cells. We explained this phenomenon through the influence of ERα on the growth of breast cancer cells, that is, ERα activation enhanced the growth of natural ERα-positive breast cancer cells, and eventually increased sensitivity to chemotherapeutic agents. However, for Bcap37 cells transformed from ERα-negative breast cancer cells, ERα activation

inhibited the growth of cancer cells, and increased the resistance of cancer cells to chemotherapeutic agents. Conclusions ERα activation was unable to induce the drug resistance of natural ERα positive T47D breast cancer cells. Although it increased the drug resistance of Bcap37 cells transformed from ERα-negative breast cancer cells, this was, however, attributable only to the inhibitory effect of E2 on the growth of these ERα-transfected Bcap37 cells. The observation was not applicable to common ERα-positive breast cancer cells. Taking together our in vitro and previous clinical findings, we indicated that, although ERα was associated with chemoresistance of breast cancers, ERα itself did not mediate this resistance process. This finding might explain why the co-application of the estrogen antagonist tamoxifen and the chemotherapeutic agents did not have good therapeutic effects in breast cancer therapy.

Methods Samples Unresectable

American Joint Committee on

Methods Samples Unresectable

American Joint Committee on Cancer Stage 3 or 4 malignant melanoma samples were obtained as part of a phase II, selleck chemicals multi-centre, open-label, parallel-group, randomised study to compare the efficacy of selumetinib (AZD6244) versus temozolomide. Locally advanced or metastatic NSCLC samples were obtained as part of a double-blind, placebo-controlled, parallel-group, multicentre, randomised, phase III study (Iressa Survival Evaluation in Lung Cancer (ISEL)) trial [17]. All patients provided written informed consent; the trials were ethically approved and performed according to principles of good clinical practice. Sample Selleck PF-3084014 processing All samples underwent a haematoxylin and eosin pathology review to confirm the presence of tumour in the samples. The NSCLC samples were macro-dissected by scraping only the tumour area that had been selected Vorinostat by a pathologist. No enrichment by macro-dissection was performed on the melanoma samples. This was because the planned primary analysis method was ARMS

and macro-dissection was thought unnecessary due to the sensitivity of the method. Genomic DNA was extracted from thin sections totalling 40 μm by digestion in proteinase K for 48 h, boiling in 5% chelex, phase-extracting in chloroform, ethanol-precipitating and resuspending in 100 μl water [18]. This method eliminated the need for a xylene de-waxing step, thus reducing potential tissue loss. The same extraction method was used for both sample sets. NSCLC DNA samples were quantified by quantitative PCR using primers and probes specific to alpha-1 antitrypsin: forward control primer AGGACACCGAGGAAGAGGACTT; reverse control

primer GGAATCACCTTCTGTCTTCATTT, control probe Cy5-CTGCLTPAZGAGGGGAA-Elle (L = LNA (locked Phloretin nucleic acid) modified C, P = LNA G, Z = LNA T). All primers and probes were manufactured by Eurogenetec. The primers were 0.1 μM and TaqMan probes at 0.5 μM. PCR was performed at 95°C for 10 min, followed by 40 cycles of 94°C for 45 s, 60°C for 1 min and 72°C for 45 s in the MX3000 (Stratagene). Data were collected at the 60°C stage of the reaction. A dilution series of known amounts of normal genomic DNA (Roche) was amplified in the same machine run and the MX3000 software extrapolated the DNA concentration of the unknown samples from the standard curve generated. This method of quantification was used rather than spectrophotometry as it only measures amplifiable DNA. Only NSCLC samples with detectable amplifiable DNA (>5 genomic copies/μl) were used for mutation analysis. Extracted melanoma DNA was not quantified prior to mutation analysis. Instead, the control reaction was used to determine DNA extraction success concurrent with the ARMS reactions.

Nanoscale Res Lett 2010, 5:1721–1762 CrossRef 14 Yue H, Jia R, C

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Dan Y, Seo K, Takei K, Meza JH, Javey A, Crozier KB: Dramatic reduction of surface recombination by in situ surface passivation of silicon nanowires. Nano Lett 2011, 11:2527–2532.CrossRef 17. Lipiski M, Ziba P, Panek P, Jonas S, Kluska S, Czternastek H, Szyszka A, Paszkiewicz B: Silicon nitride XAV-939 purchase for silicon solar cells. In Proceedings of the 29th International Conference of IMAPS 2005: September 19–21 2005; Darłówko. Washington, D.C.: International Microelectronics and Packaging Society; 2005:203–206. 18. Li H, Jia R, Chen C, Xing Z, Ding W, Meng Y, Wu D, Liu X, Ye T: Influence of nanowires length on performance of crystalline silicon solar cell. Appl Phys Lett 2011, 98:116–118. 19. Tanaka M, Taguchi

M, Matsuyama T, Sawada T, Tsuda S, Kinase Inhibitor Library cost Nakano S, Hanafusa H, Yukinori Kuwano Y: Development of new a-Si/c-Si heterojunction solar cells: ACJ-HIT (artificially constructed junction-heterojunction with intrinsic thin-layer). Jap J Appl Phys 1992, 31:3518–3522.CrossRef 20. Rath JK, Rubinelli FA, Van der Werf CHM, Schropp REI, Van der Weg FW: Performance of heterojunction p + microcrystalline silicon n crystalline silicon solar cells. J Appl Phys 1997, 82:6089–6095.CrossRef 21. Terada N, Tsuge S, Toshiaki B, Takahama T, Wakisaka K, Tsuda S, Nakano S: High-efficiency a-Si/c-Si heterojunction solar cell photovoltaic energy conversion. In Proceedings of the 24th IEEE Photovoltaic Specialists Conference: December 5–9 1994; Waikoloa. Piscataway: IEEE; 1994:1219–1226. 22. Knights CJ, Lujan AR: Microstructure of plasma-deposited a-Si : H films. Appl Phys

Lett 1979, 35:244–246.CrossRef 23. Bandaru RP, Pichanusakorn P: An outline of the synthesis and properties Urease of silicon nanowires. Semicond Sci Technol 2010, 25:1–16. 24. Mahan HA, Molenbroek CE, Gallagher CA, Nelson PB, Iwaniczko E, Xu Y: Deposition of device quality, low hydrogen content, hydrogenated amorphous silicon at high deposition rates. US Patent 6,468,885 B1, 9 Oct 2002 25. Xie ML, Qi WM, Chen MJ: The nature of several intense Si-H infrared stretching peaks in the neutron-transmutation-doped Si-H system. J Phys Condens Matter 1991, 3:8519–8523.CrossRef 26. Tsai CC, Fritzsche H: Effect of annealing on the optical properties of plasma deposited amorphous hydrogenated silicon. Sol En Mater 1979, 1:29–42.CrossRef 27.

J Med Microbiol 2003, 52:337–344 PubMedCrossRef 34 Salloum M, va

J Med Microbiol 2003, 52:337–344.PubMedCrossRef 34. Salloum M, van der Mee-Marquet N, Domelier AS, Arnault L, Quentin R: Molecular characterization and prophage DNA contents of Streptococcus agalactiae strains isolated from adult skin and osteoarticular infections. J Clin Microbiol 2010, 48:1261–1269.PubMedCrossRef 35. Agnew W, Barnes AC: Streptococcus iniae:

an aquatic pathogen of global veterinary significance EX527 and a challenging candidate for reliable vaccination. Vet Microbiol 2007, 122:1–15.PubMedCrossRef 36. Haguenoer E, Baty G, Pourcel C, Lartigue MF, Domelier AS, Rosenau A, et al.: A multi locus variable number of tandem JNK-IN-8 research buy repeat analysis (MLVA) scheme for Streptococcus agalactiae genotyping. BMC Microbiol 2011, 11:171.PubMedCrossRef 37. Elliott JA, Facklam RR, Richter CB: Whole-cell protein patterns of nonhemolytic group B, type Ib, streptococci isolated from humans, mice, cattle, frogs, and fish. J Clin Microbiol 1990, 28:628–630.PubMed 38. Evans JJ, Pasnik DJ, Klesius PH, Al-Ablani S: First report of Streptococcus agalactiae and Lactococcus garvieae from a wild bottlenose dolphin

(Tursiops truncatus). J Wildl Dis 2006, 42:561–569.PubMed 39. Lartigue MF, Héry-Arnaud G, Haguenoer E, Domelier AS, Schmit PO, Mee-Marquet N, et AC220 nmr al.: Identification of Streptococcus agalactiae isolates from various

phylogenetic lineages by matrix-assisted laser desorption ionization-time of flight mass filipin spectrometry. J Clin Microbiol 2009, 47:2284–2287.PubMedCrossRef 40. Baker JR: Further studies on grey seal (Halichoerus grypus) pup mortality on North Rona. Br Vet J 1988, 144:497–506.PubMedCrossRef 41. Baker JR, McCann TS: Pathology and bacteriology of adult male Antarctic fur seals, Arctocephalus gazella, dying at Bird Island. South Georgia. Br Vet J 1989, 145:263–275.CrossRef 42. Miranda C, Gamez MI, Navarro JM, Rosa-Fraile M: Endocarditis caused by nonhemolytic group B streptococcus. J Clin Microbiol 1997, 35:1616–1617.PubMed 43. Nickmans S, Verhoye E, Boel A, Van VK, De BH: Possible solution to the problem of nonhemolytic group B streptococcus on Granada medium. J Clin Microbiol 2012, 50:1132–1133.PubMedCrossRef 44. Lopez-Sanchez MJ, Sauvage E, Da CV, Clermont D, Ratsima HE, Gonzalez-Zorn B, et al.: The highly dynamic CRISPR1 system of Streptococcus agalactiae controls the diversity of its mobilome. Mol Microbiol 2012, 85:1057–1071.PubMedCrossRef 45. Verner-Jeffreys DW, Baker-Austin C, Pond MJ, Rimmer GS, Kerr R, Stone D, et al.: Zoonotic disease pathogens in fish used for pedicure. Emerg Infect Dis 2012, 18:1006–1008.PubMedCrossRef Competing interests The authors declare that they have no competing interests.

Patients diagnosed with ‘indeterminate colitis’ were excluded fro

Patients diagnosed with ‘indeterminate colitis’ were excluded from this study. All included patients were screened for vitamin D deficiency at the end of summer 2009 (September–November) and winter 2009–2010 (January–March) at the gastroenterology outpatient department of a large teaching hospital in the centre

of the Netherlands. Written informed consent was obtained from all participants. The study protocol was approved by the local Medical Ethics Committee of the Meander Medical Centre. Data collection A standardized questionnaire was used to analyse information on self-reported demographic data i.e. age, sex, ethnicity, health behaviour, physical activity, check details current smoking and alcohol usage. Physical activity was assessed using the SQUASH (Short QUestionnaire selleck chemicals llc to ASess Health) questionnaire according to the national physical activity scale [12]. Excessive alcohol usage was defined as >21 alcoholic units per week for men and >14 alcoholic units per week for women. Disease activity of IBD was assessed by the Manitoba IBD index

[13]. This index is based on patient self-reports enclosing IBD-related symptoms in the last 6 months. Other patient characteristics were retrieved from documented medical records in order to obtain data of fractures in the past and corticosteroid usage. Body mass index was measured by calculating weight Axenfeld syndrome in kilograms divided by the square height in meters. For their vitamin D assessment, patients had to undergo serum 25OHD measurement at the end of summer and winter and complete two questionnaires. In these questionnaires, patients were asked to report their daily oral vitamin

D supplementation (including daily dosages and type of supplementation i.e. prescription medication and/or over the counter supplements), medication Fosbretabulin order compliance, preferred exposure to sunlight or shade when outdoors and average number of days per week with >2 midday hours exposure to sunlight during summer. Furthermore, sun holidays in the last 6 months, frequency of solarium visits, calcium intake (dairy products /day) and intake of fatty fish (servings/month), i.e. mackerel, herring and salmon, were assessed. Laboratory measurements Original serum samples were drawn in EDTA, respectively, heparin-containing collection tubes, centrifuged and stored at −30°C. Biochemical and haematological laboratory markers (e.g. haemoglobin (Hb), haematocrit (Ht), red blood cell distribution width (RDW), erythrocyte sedimentation rate (ESR), C-reactive protein (CRP), calcium, phosphate, alkaline phosphatase, albumin, creatinine and thyroid stimulating hormone) were measured at the end of summer (September–November 2009).

[18] The strains were grown in 79CA to an OD600 of ~0 6, washed

[18]. The strains were grown in 79CA to an OD600 of ~0.6, washed SRT1720 nmr twice in sterile water, and resuspended in 25 mM phosphate buffer (pH 6.8) to a final OD600 of 0.06. 200 μl of a bacterial suspension was placed onto a slide with modified Fåhraeus medium Ion Channel Ligand Library nmr containing a sterile germinated clover seedling with root ~2 cm long. The slides were incubated for 90 min at room temperature, and root attachment of tested strains

was observed under confocal laser scanning microscopy. To study plant root invasion by the Rt2472 and the Rt24.2, clover seedlings ~2 cm long were placed on the top of microscope slides, which were previously covered with 2 ml Fåhraeus agar, and inoculated with 100 μl of bacterial suspension in sterile water of OD600 of 0.08 [42]. The slides with seedlings were placed in 50-ml culture tubes containing 5 ml of liquid Fåhraeus medium and covered loosely by sterile Whatman paper. To determine the efficiency of Tipifarnib mw invasion, 25 plants inoculated with the particular strain were examined after 3, 4, 6, 8, and 10 days. To determine quantitatively adhesion efficiency and the growth rate on clover

roots by the Rt2472 and Rt24.2, the methods described by Fujishige et al. 2006 [78] were applied. For adhesion assay, three-day-old seedlings were inoculated by dipping their roots into bacterial suspensions of OD600 of 0.08 for 30 min or placed on Fåhraeus agar medium plates, inoculated by bacterial suspensions of OD600 of 0.08 (100 μl per seedling), and incubated for two days. The seedlings were placed on sterile Whatman paper to remove the excess of liquid, and subsequently were grown on Whatman paper wetted with liquid Fåhraeus

medium for 48 h. Next, roots were washed overnight with sterile water containing 0.05% Tween-20 on a rocking platform shaker to remove loosely associated cells. After removing the excess of liquid, the roots were weighed. To determine the number of attached bacteria, the root of each seedling was homogenized in 300 μl of water and root homogenate was plated in dilutions on 79CA plates for colony counting. Acknowledgements This research has been supported by the grant from the Ministry of Science and Higher Education no. N N303 092234. C-X-C chemokine receptor type 7 (CXCR-7) The authors would like to thank Prof. Teresa Urbanik-Sypniewska for help in the preparation and analyses of EPS and LPS. We thank Mrs Maria Małek for technical assistance. Electronic supplementary material Additional file 1: Figure S1 – Western blotting analysis of membrane and extracellular protein fractions of the R. leguminosarum wild type and the rosR mutant (Rt2472) with polyclonal antisera against PssB (A) and PssN (B). The migration positions of molecular mass markers are shown. Lines 1-6: extracellular protein fractions isolated from 10 ml of: Rt24.2 TY culture supernatant (1), Rt2472 TY culture (2), Rt24.2 M1 culture (3), Rt24.