This growth phase of Aspergillus fumigatus is inhibited by lactoferrin-mediated iron depletion [28]. In contrast, inhibition of the hyphal form of Aspergillus fumigatus requires NADPH oxidase [28, 30]. Aspergillus selleck screening library nidulans lacking the catalase genes are capable of causing disease in gp47phox KO mice, which suggested that reactive oxygen intermediates

might not be inhibiting the organism directly [30]. It has been suggested that activation of intracellular proteases by reactive oxygen intermediates is important for killing Candida and several types of bacteria [31]. There is one report that administration of pentraxin 3 protected gp47phox mice from experimental Aspergillus fumigatus infection, suggesting that this molecule in important for resistance to Aspergillus fumigatus and may be lacking in CGD mice [32]. The only evidence that primary pathogenic fungi are more virulent in CGD mice is a study with Sporothrix schenckii [33]. These investigators found that gp91phox KO mice infected with Sporothrix schenckii intradermally died within three months, whereas control mice survived this infection. They also found that PMN from gp91phox KO mice were not able to control the growth of Sporothrix schenckii as well as the controls. We have not been able to find any published data on Blastomyces dermatitidis, C. immitis or

Histoplasma capsulatum Vistusertib experimental infections in CGD mice. People with chronic granulomatous disease have increased susceptibility to Aspergillus infections and, to a lesser extent, infections due to other opportunistic fungi [34]. There have been no reports of increased susceptibility to the primary pathogenic fungi Coccidioides, Histoplasma

capsulatum, Blastomyces dermatitidis or Sporothrix schenckii. One expert states that these infections are not a problem in chronic granulomatous disease [34]. One CGD patient has been observed to recover uneventfully from pulmonary coccidioidomycosis without anti-fungal therapy (J. Galgiani, Sclareol personal communication). The observation that NADPH oxidase is not required for a protective immune response to experimental coccidioidomycosis raises the question of what immune mechanisms used to kill spherules and endospores in vivo. One potential protective immune effector mechanism is oxidative stress due to nitric oxide. We have previously reported that IL-10 exacerbates the course of experimental coccidioidomycois and inhibits nitric oxide synthase [35]. On the other hand, a very recent study suggests that Coccidioides is resistant to killing by NO and that mice with a deletion mutation in inducible nitric oxide synthase are able to kill Coccidioides [36]. Coccidioides spherules can be very large (more than 60 μM in diameter) and therefore difficult to phagocytose. Perhaps inhibiting the growth of the endospore Selonsertib mw controls the growth of the organism. Understanding the mechanisms of protective immunity is important for optimally preventing and treating infections with this pathogenic fungus.

Phys Rev B 2005, 71:125309.CrossRef 24. Buyanova IA, Chen WM, Pozina G, Bergman JP, Monemar B, Xin HP, Tu CW: Mechanism for low-temperature photoluminescence in GaNAs/GaAs structures grown by molecular-beam epitaxy. Appl Phys Lett 1999, 75:501–503.CrossRef 25. Kudrawiec R, Sek G, Misiewicz J, Li LH, Harmand JC: Investigation of recombination processes involving defect-related states in (Ga, In)(As, Sb, N) compounds. Eur Phys J Appl Phys 2004, 27:313–316.CrossRef 26. Kaschner A, Lüttgert T, Born H, Hoffmann A,

Egorov AY, Riechert H: Recombination mechanisms in GaInNAs/GaAs multiple Temsirolimus in vitro quantum wells. Appl Phys Lett 2001, 78:1391–1393.CrossRef 27. Baranovskii SD, Eichmann R, Thomas P: Temperature-dependent exciton luminescence in quantum wells by computer simulation. Phys Rev B 1998, 58:13081–13087.CrossRef

Z-IETD-FMK chemical structure 28. Mair RA, Lin JY, Jiang HX, Jones ED, Allerman AA, Kurtz SR: Time-resolved photoluminescence studies of In x Ga 1-x As 1-y N y . Appl Phys Lett 2000, 76:188–190.CrossRef 29. Zu LQ, Lin JY, Jiang HX: Dynamics of exciton localization in a CdSe 0.5 S 0.5 selleckchem mixed crystal. Phys Rev B 1990, 42:7284–7287.CrossRef 30. Ouadjaout D, Marfaing Y: Thermal activation of localized excitons in Zn x Hg 1-x Te semiconductor alloys: photoluminescence line-shape analysis. Phys Rev B 1992, 46:7908–7910.CrossRef 31. Cho Y-H, Song JJ, Keller S, Minsky MS, Hu E, Mishra UK, DenBaars SP: Influence of Si doping on characteristics of InGaN/GaN multiple quantum wells. Appl Phys Lett 1998, 73:1128–1130.CrossRef 32. Cho Y-H, Gainer GH, Fischer AJ, Song JJ, Keller S, Mishra UK, DenBaars SP: “”S-shaped”" temperature-dependent emission shift and carrier dynamics in InGaN/GaN multiple quantum Nitroxoline wells. Appl Phys Lett 1998, 73:1370–1372.CrossRef 33. Lin YC, Chung HL, Chou WC, Chen WK, Chang WH, Chen CY, Chyi

JI: Carrier dynamics in isoelectronic ZnSe 1-x O x semiconductors. Appl Phys Lett 2010, 97:041909.CrossRef 34. Gourdon C, Lavallard P: Exciton transfer between localized states in CdS 1–x Se x alloys. Phys Status Solidi B 1989, 153:641–652.CrossRef 35. Rubel O, Baranovskii SD, Hantke K, Kunert B, Rühle WW, Thomas P, Volz K, Stolz W: Model of temperature quenching of photoluminescence in disordered semiconductors and comparison to experiment. Phys Rev B 2006, 73:233201.CrossRef 36. Rubel O, Galluppi M, Baranovskii SD, Volz K, Geelhaar L, Riechert H, Thomas P, Stolz W: Quantitative description of disorder parameters in (GaIn)(NAs) quantum wells from the temperature-dependent photoluminescence spectroscopy. J Appl Phys 2005, 98:063518–063518. –7CrossRef 37. Grüning H, Kohary K, Baranovskii SD, Rubel O, Klar PJ, Ramakrishnan A, Ebbinghaus G, Thomas P, Heimbrodt W, Stolz W, Rühle WW: Hopping relaxation of excitons in GaInNAs/GaNAs quantum wells. Phys Status Solidi C 2004, 1:109–112.CrossRef 38.

Because the stress-induced expression of fbp1 + and pyp2 + genes is positively regulated by Sty1 via Atf1, we considered the possibility that the delayed expression of both genes in pmk1Δ cells during the shift

to a non-fermentable carbon source might result from an altered kinetics in the activation of the SAPK pathway. Therefore, we comparatively analyzed Sty1 phosphorylation during glucose deprivation in control versus pmk1Δ cells. As shown in Figure  LY3023414 cell line 5D, glucose withdrawal induced a quick activation of Sty1 in control cells that was maintained and slowly decreased after 3-4 hours in the presence of non-fermentable carbon sources. However, the kinetics of Sty1 activation in pmk1Δ cells was clearly altered, with a more pronounced dephosphorylation after the initial activation, and the activation Gemcitabine mw maintained for longer times (Figure  5D). Similarly, despite a decreased mobility shift and expression observed

early after transfer from fermentative to respiratory medium, Atf1 protein levels (expressed as a genomic copy of the atf1 + gene tagged with two copies of the HA epitope and six histidine residues) remained high in pmk1Δ cells at longer incubation times as compared to control cells (Figure  Methisazone 5E). Notably, the late activation of both Sty1 and Atf1 prompted in the absence of Pmk1 is in good agreement with the delayed expression pattern observed for Fbp1 or Pyp2 (Figures  5B and C). Taken together, these results suggest that in fission yeast Pmk1 positively regulates the Gefitinib solubility dmso timely activation of the SAPK pathway during the switch from fermentative to respiratory metabolism. Discussion Several lines of evidence obtained in this work strongly suggest that the signal for glucose exhaustion is channelled to the Pmk1 MAPK module through a mechanism involving unknown elements.

While Rho2 GTPase is fully or partially involved in Pmk1 activation in response to most environmental stresses [18], stimulation of the MAPK cascade in response to glucose withdrawal is barely dependent on the activity of this GTPase, since in Rho2-less cells Pmk1 is activated similar to wild type cells except for a slower kinetics at earlier times after carbon source depletion. Lack of function or dominant negative mutants in Rho GTPases like Rho5, whose expression is heavily induced after nutrient deprivation [24], and in Rho1 or Cdc42, which have been mentioned as potential upstream activators of this signaling pathway [17, 20], were able to activate Pmk1 in response to this nutritional stress.

EpCAM+ or HER2/neu+: > 10% stained cells in autologous tumor cell preparations; CUP = carcinoma of unknown primary. Application of trAb and monitoring All nine patients received i.p. trAb applications. No dose escalation for the third application was performed in www.selleckchem.com/products/pnd-1186-vs-4718.html patient A because of side effects. In patient C, reduced starting dose of 5 μg was in respect of a body weight of 43 kg only; Patient F refused the third application of trAb. For detailed

therapy of each patient, please see Table 2 and Table 3. Table 2 I.p. application of trAb CP673451 in vivo anti-EpCAM and side effects Pat. TrAb anti-EpCAM therapy (μg i.p./day) Cumulative dose Side effects   μg day μg day μg day (μg)   A 10 1 20 5 20 9 50 Elev. of AP (3), γ-GT (4); fever (3); abdominal pain (3); vomiting (3) B 10 1 20 6 40 9 70 Elev. of AP (2), bilirubin (2), γ-GT (3), GOT (3), GPT (3); fever (3); abd. pain (3); vomiting (2); allergic exanthema OICR-9429 (2) C 5 1 20 3 40 7 65 Fever (2) F 10 1 20 5 –   30 Elev. of AP (2), PTT (2), GPT (3); fever (1); abdominal pain (3); vomiting (2) G 10 1 20 5 40 10 70 Elev. of AP (1), bilirubin (2), γ-GT (3), GPT (3); fever (1); abdominal pain (3) H 10 1 20 7 40 13 70 Elev. of AP (1), bilirubin (2), gGT (3), creatinine (2); fever (1); abdominal pain (3) I 10 1 20 8 40 12 70 Elev. of AP (1); fever (2); vomiting (3) Table 3 I.p. application

of trAb anti-Her2/neu and side effects Pat. TrAb anti Her2/neu therapy (μg i.p./day) Cumulative dose Side effects   μg Day μg Day μg day (μg)   D 10 1 40 4 80 8 130 Fever (1) E 10 1 40 6 80 8 130 Fever (1); abdominal pain (2) Individual schedule of trAb therapy and side effects according to the National Cancer Institute (NCI) common toxicity criteria. TrAb treatment was accompanied by transient fever (up to 40.4°C) after 9 applications. The fever developed

six to ten hours after trAb infusion and disappeared within the next day. Metamizole (1000 mg) was given in these cases. Six patients complained about abdominal pain; four patients had vomiting and required treatment with Dimenhydrinate. No patient required ICU admittance. Atezolizumab supplier Elevated liver enzymes, elevated levels of γ-glutamyl transferase and alkaline phosphatase were observed after trAb application. These laboratory changes disappeared spontaneously within the treatment intervals. TrAb treatment was followed by an elevation of serum levels of IL-6, TNF-α, and soluble IL-2 receptor one day after treatment. The slight decrease on the second day after every trAb application was statistically not significant (Figure 1A, 1B). The inflammatory cytokine IL-6 showed a substantial increase after the first trAb infusion only; despite trAb dose escalation there were only moderate increases after the following two applications (Figure 1C).

Interestingly, caspase-3 activity was not observed in Aspc1 cells (Additional file 3 figure S3C), a cell line with less sensitivity to PB282 (Additional file 3 figure S3D). Figure 7 Caspase-3 inhibition by lipophilic antioxidant correlates with caspase dependence. (A) Caspase-3 inhibition by the hydrophobic antioxidant α-tocopherol

(α-toco), hydrophilic antioxidant N-acetylcyteine (NAC), or caspase-3 inhibitor DEVD-FMK (1 μM) in Bxpc3 cells following 24 hour treatment with SW43 (30 μM), PB282 (90 μM), or HCQ (90 μM). Data represents normalized inhibition compared to CH5183284 datasheet caspase-3 inducing treatment, n = 3, p < 0.05. (B) Cell viability following 24 hour treatment with SW43 or PB282 in the presence of α-toco or NAC. Data represents percent viability compared to DMSO

treated cells, n = 3, * p < 0.05. Discussion Recent synthesis of fluorescently labeled analogs of SV119 (SW120) and PB28 (PB385), allowing live cell imaging, has buy LY2835219 shown check details sigma-2 receptor ligand subcellular localization to the membrane components of the cell ultrastructure [16, 17]. In various pancreatic cancer cell lines we have observed similar results, and hypothesized that strong uptake into the endo-lysosomal compartment induces lysosomal membrane permeabilization (LMP). In addition, weakly basic amines as a class of drugs have Fenbendazole been shown to induce LMP [24] and cell death [25], and the amine groups present on sigma-2 receptor ligands suggest they can induce LMP. We examined here whether this could influence the caspase-3 activation in pancreatic cancer we observed earlier [8–10] and found that LMP occurs shortly following treatment with a variety of structurally diverse

sigma-2 receptor ligands, verified by both AO and LysoTracker release from the lysosome. Uptake of fluorescently labeled compounds was inhibited by blocking the lysosomal pH gradient with concanamycin A (CMA), a specific inhibitor of the V-Type ATPase [26, 27], and translated into significant viability protection following treatment. SW43 was a stronger inducer of LMP, with greater protection from CMA pretreatment than for PB282. This that some sigma-2 receptor ligands have a greater propensity to influence the lysosomal death pathway Chemical structure differences may be responsible for this difference. For instance, the structure of the N-(9-(6-Aminohexyl)-9-azabicyclo[3.3.1]-nonan-3α-yl)-N-(2-methoxy-5-methylphenyl) carbamate hydrochloride (SV119) derivatives contain an alkyl extension with terminal amine group that is not present in the 1-cyclohexyl-4-[3-(5-methoxy-1,2,3,4-tetrahydro-naphthalen-1-yl)-propyl]-piperazine dihydrochloride (PB28) derivatives, a moiety that increases lysosomal membrane insertion and permeabilization [28].

SP, SZ, AG, DF and DP participated in the experiments of cell culture and molecular biology. MM participated in statistical analysis and interpretation. SN, NS and AS participated in the design of the experiments. All authors read and approved the final manuscript.”
“Introduction Invasive ductal carcinoma is the most common breast

malignancy and a leading cause of cancer-related death in women worldwide.[1] Despite developments in surgical methods, cytotoxic chemotherapy, and agents targeted against estrogen receptor (ER) and HER2, a subset of patients with advanced stage invasive ductal carcinoma may experience tumor recurrence or metastasis within several years after treatment. It has been estimated that 11% of women with invasive ductal carcinoma will experience a

https://www.selleckchem.com/products/Trichostatin-A.html recurrence within five years after surgery, including 8% of women with luminal A breast cancers and 15% of women with tumors having basal-like features.[2, 3] The cancer stem cell hypothesis was proposed to explore breast cancer heterogeneity and the risk of breast cancer recurrence, and these cell subpopulations may contribute to drug resistance that drives tumor recurrence or metastasis [4]. Using keratin profiling, Hoechst dye efflux, and flow cytometry analysis of cell surface markers such as CD44, CD24, CD133, epithelial cell adhesion molecule, and mucin-1,[5] normal human breast stem-cell like cells have been independently identified GS-4997 manufacturer as showing elevated expression of CD44 and no expression of CD24 (CD44+/CD24-), as well as elevated levels of stem cell enriched genes.[6] The CD44+/CD24- subpopulation Interleukin-2 receptor was believed

to be putative stem cells in human breast tissue, enriched for basal cells and motility genes, which could be generated during the epithelial-mesenchymal transition. Moreover, these cells were negative for mucin 1, estrogen receptor (ER), and v-erb-b2 erythroblastic leukemia viral oncogene homolog 2 (erbB2) receptor.[7, 8] More importantly, high expression of CD44+/CD24- cancer cells was associated with poor patient prognosis.[9] These cells had the phenotype of cancer cells during the epithelial to mesenchymal transition, [10] indicating that the gene expression pattern of CD44+/CD24- cells in breast cancers resembled more closely the pattern observed in CD44+/CD24- cells in normal breast than that of CD44-/CD24+ cells isolated from the same tumor.[6] Taken together, these findings indicated that CD44+/CD24- cells, especially those expressing epithelial cell adhesion molecule, were breast cancer stem cells (CSCs).[11] In contrast, breast cancer cells expressing elevated levels of aldehyde dehydrogenase 1 (ALDH1) were also described as breast CSCs, with ALDH1+/CD44+/CD24- cells displaying strong tumorigenic potential.[12] Moreover, breast CSCs were believed to constitute up to 35% of the cancer cells in a tumor, whereas these cells Cell Cycle inhibitor constituted only about 1% of stem and progenitor cells present in normal breast [13].

OPN was mixed with either AOM1

or control antibody. Antibody concentrations Avapritinib purchase were titrated from 10 μM in a three-fold dilution series to approximately 0.1 nM. Human OPN and test antibody were pre-incubated for 1 hour at room temperature on a rotary mixer before being applied to the αVβ3 coated ELISA plates. After a washing step (3 times with Buffer 1 + 0.05% Tween-20 and three times with Buffer 1 alone), rabbit polyclonal anti-human OPN antibody (O-17, IBL, Japan) was added to the plates (100 μl/well) at a concentration of 4 μg/ml for 1 hour at room temperature. Plates were then washed (3 times with Buffer 1 + 0.05% Tween-20 and 3 times with Buffer 1 alone) and goat-anti-rabbit antibody (Fc specific) HRP selleck compound Conjugate (Jackson Immunoresearch, PA) was added to each well (100 μl/well, 1 in 5000 dilution in Block Buffer) for 1 hour at room temperature. Following final washes (3 times with Buffer 1 + 0.05% Tween-20 and 3 times with Buffer 1 alone) ELISA was developed with 100 μl/well

BM Blue POD substrate (Roche, NJ) and the selleckchem colorimetric reaction was stopped with 100 ul/well 0.2 M H2SO4. Absorbance at 450 nm was measured using a Spectromax plate reader (Molecular Devices, CA) and analysis was conducted using Microsoft Excel Data-Analysis Add-In fitting IC50 curves to a 4-paramter sigmoidal saturation binding model. Selectivity of AOM1 for OPN EIA/RIA plates (Corning, NY) were coated with 1 mg/ml of RGD-motif containing Methane monooxygenase protein which included OPN, Thrombospondin, Vitronectin, ColIAI or Fibronectin (R&D Systems, MN) in Buffer 1 (PBS pH 7.2 containing 2 mM MgClR2R and 0.2 mM MnClR2R for 16 hours at 4°C). Plates were washed three times with Buffer 1 and were blocked with commercially available Blocking buffer (3% BSA (Rockland, PA) in Buffer 1) followed by washing three times with Buffer 1 and AOM1 was added at 0, 0.1, 1, 10, and 1000 nM in blocking buffer, and incubated at RT for 1 hr. Plates were washed (3 times with Buffer 1 + 0.05% Tween-20 and three times with

Buffer 1 alone). Goat Anti-Human IgG (Fc) Peroxidase Conjugate (Jackson Immunoresearch, PA) was added (1 in 5000 in block buffer) and plates were incubated at RT for 1 h followed by a wash (3 times with Buffer 1 + 0.05% Tween-20 and three times with Buffer 1 alone). BM Blue Solution (Roche, NJ) was used to develop the assay and quenched with 0.18 M HR2RSOR4R. Absorbance at 450 nm was detected using a Spectramax plate reader (Molecular Devices, CA) and data were analyzed using Microsoft Excel. Characterization of AOM1 Fab binding to OPN Binding of Fab fragment of AOM1 to recombinant OPN was determined using surface plasmon resonance (SPR) analysis on a Biacore 3000 instrument (GE Healthcare, CA).

These results open the door for the use of continuous chlorophyll a fluorescence measurements, which are becoming increasingly available (e.g. Pintado et al. 2010; Büdel et al. 2014), to estimate the productivity of biocrusts, an important process that, however, is difficult to measure in the field (Raggio et al. 2014). The last two articles of this special issue are devoted to two key biocrust constituents: cyanobacteria

and green algae. Williams et al. (2014) studied how cyanobacteria responded to rehydration during the dry season in the Boodjamulla National Park (Australia). They found that cyanobacteria did not recover PSII activity or CO2 uptake after a rehydratation following a 125 day drought #selleck chemical randurls[1|1|,|CHEM1|]# in 2009. Although new colonies of Nostoc grew, other cyanobacteria remained inactive, even though liverworts and lichens in the same biocrust community had responded within 24 h. The authors also collected cyanobacterial crusts during the dry season in 2010, then reintroduced them into their natural environment and exposed to rainfall during the 2011 wet season. Within 24 h, PSII in cyanobacteria

from a range of crust types had resurrected, and their CO2 uptake was verified. These results contrast with the widely accepted view that terrestrial cyanobacteria are drought tolerant MK-1775 in vitro and rapidly recommence photosynthesis once moisture is available, and indicate that cyanobacterial function appears to be controlled by environmental conditions other than rainfall during the dry season. In the last article in this special issue, Karsten and Holzinger (2014) review the acclimation strategies against ultraviolet radiation and dehydration of green algae, which is a major component

of biocrusts, particularly in alpine habitats. These organisms serve as good model organisms to study desiccation tolerance or photoprotective mechanisms, due to their natural capacity to withstand unfavorable conditions. The authors point out the urgent need for modern phylogenetic approaches in characterizing these organisms, and molecular methods for analyzing the metabolic changes involved in their adaptive strategies. Due to the large number of topics being investigated by biocrust Reverse transcriptase researchers, this special issue cannot provide a complete, definitive overview of this body of research. Each of the topics treated in the different articles included would certainly require a special issue by itself, and some, such as the effects of biocrusts on nitrogen cycling (e.g. Belnap 2002; Barger et al. 2005; Delgado-Baquerizo et al. 2010, 2013; Hu et al. 2014), are underrepresented here due to limitations of space. The diverse contributions included in this theme issue are, however, timely and we hope that they will advance our understanding of the important ecological roles played by biocrusts in the ecosystems where they are present, stimulate further research on these important organisms, and increase the awareness of conservationists to the importance of these systems.

0 (1.0, 1.1) 1.0 (1.0, 1.1) \( t_E_\hboxmax \) INR (h) 24.0 (8.0–36.0) 24.0 (4.0–36.0) E max INR (fraction) 1.7 (1.5, 1.9) 1.9 (1.6, 2.2) AUCINR (fraction × h) 38.5 (30.1, 49.2) 38.8 (30.9, 48.8) Baseline factor VII (%) 82.6 (70.7, 96.5) 86.9 (71.3, 106) \( t_E_\hboxmax \) factor VII (h) 36.0 (24.0–36.0) 24.0 (24.0–36.0) E max factor VII (%) 16.1 (12.1, 21.4) 17.1 (12.7, 23.1) AUCfactor VII (% × h) 3,368 (2,676, 4,241) 3,281 (2,226, 4,835) Data are geometric means (and 95 % confidence limits) or, for selleck kinase inhibitor t max, the

median (and range) AUC area under the plasma concentration–time curve,

E max maximum effect, INR find more international normalized ratio Following administration of warfarin, both in the absence and presence of almorexant, factor VII concentrations decreased (Fig. 3). The maximum decrease occurred 24–36 h after administration, and factor VII slowly returned to baseline thereafter. The pharmacodynamic analysis appeared to show a difference in the time to E max between treatments, i.e., 36 h for treatment A and 24 h for treatment B, whereas other variables were similar (Table 3). Fig. 3 Arithmetic mean (and standard Selleckchem MLN0128 deviation) plasma concentration–time Progesterone profile of factor VII after administration of a single dose of 25 mg warfarin alone (treatment B) and in the presence of almorexant 200 mg once daily for 10 days with a single dose of 25 mg warfarin on day 5 (treatment A) to healthy male subjects (n = 13) 4 Discussion Almorexant is a dual orexin receptor antagonist and has been shown in vitro to inhibit CYP2C9, CYP2D6, and CYP3A4 (Actelion Pharmaceuticals, data on file). The present study investigated the effects of almorexant on warfarin pharmacokinetics and pharmacodynamics

in a randomized, two-way crossover study. Such a design reduces variability as each subject serves as his own control, thereby reducing the number of subjects to be included and is in accordance with current guidelines for in vivo interaction studies [20]. Warfarin was administered when almorexant concentrations were in steady state and any possible inhibition of CYP isoenzymes was maintained during the elimination phase of warfarin by continued administration of almorexant. The pharmacokinetics of warfarin in the absence of almorexant were in good agreement with previously reported results [19, 21].

PubMedCrossRef 50. Sohaskey CD, Zuckert WR, Barbour AG: The extended promoters for two outer membrane lipoprotein genes of Borrelia spp. uniquely include a T-rich region. Mol Microbiol 1999,33(1):41–51.PubMedCrossRef 51. Hodzic E, Tunev S, Feng S, Freet KJ, Barthold SW: Immunoglobulin-regulated expression of Borrelia burgdorferi

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