Patients were also excluded if they had taken intravenous bisphosphonates within 12 months prior to the screening visit, or strontium ranelate or fluoride at therapeutic doses (≥20 mg/day) for more than 3 months in the 2 years prior to randomization, CFTR activator or for more than a total of 2 years, or at any dosages within the 6 months prior to randomization. Previous treatment for any duration with calcitonin, oral bisphosphonates, or active vitamin D3 analogues

that had been stopped prior to or at the randomization visit was allowed. All patients provided written informed consent. Biochemical markers of bone turnover Serum concentrations of two BTMs were measured at baseline and at 3, 6 and 18 months of treatment: (1) the bone formation GDC-941 marker PINP and (2) the bone resorption marker C-terminal cross-linked telopeptides of type I collagen

(CTx). Fasting blood samples (10 ml) were collected in the morning, then serum samples were prepared and stored at −20 °C or lower at the study site for up to 4 months before being sent to a central laboratory (Covance, Geneva, Switzerland) for storage at −80 °C and processing. All samples from an individual were assayed in a single analytical batch. Serum intact PINP was measured by the Intact UniQ RIA assay (Orion Diagnostica, Espoo, Finland). This assay is not sensitive to the small molecular weight degradation products of the pro-peptide (cross-reaction only 1.2 %). The inter-assay this website (within day) analytical coefficient of variation (CV) was less than 3.1–8.2 % over the reference interval. Serum CTx was measured by the Serum Crosslaps® ELISA (Nordic Bioscience Diagnostics, Herlev, Denmark). The inter-assay CV was 5.4–11.4 %. High-resolution quantitative CT and FEA CT scans were performed at baseline and at 6 and 18 months of treatment. To optimize image quality

serving as the input data for FE analyses, we used an HRQCT protocol rather than a standard QCT protocol with thicker slices and lower plane resolution. All HRQCT assessments performed in this study have been described elsewhere [30, 37], and are briefly summarized below. A thin-slice spiral CT of the 12th thoracic vertebra (T12) was acquired using a scanner set at 120 kV and 360 mA s. If T12 was fractured, the HRQCT was performed on an intact L1 vertebra. Two images were reconstructed. The first one had a large field of view (FOV), included the patient and calibration phantom, and was used to calibrate the second image on which all analyses were carried out. The second image, with a smaller FOV size of 80 or 96 mm (pixel sizes of 0.156 or 0.188 mm) depending on the scanner type, included only the vertebra. In this latter image, the complete vertebral body was segmented using a semi-automatic algorithm.

Cell 2007, 26:415. 25. Zhao X, Scott SA, Huang M, Peng W, Kiefer AM, Flack FS, Savage DE, Lagally MG: Influence of surface properties on the electrical conductivity of silicon nanomembranes. Nanoscale Res Lett 2011, 6:402.CrossRef 26. Liu IS, Lo HH, Chien CT, Lin YY, Chen CW, Chen YF, Su WF, Liou SC: Enhancing photoluminescence quenching and photoelectric properties of CdSe quantum dots with hole accepting ligands. J Mater Chem 2008, 18:675.CrossRef 27. Zhu CQ, Wang P, Wang X, Li Y: Facile phosphine-free synthesis of CdSe/ZnS core/shell nanocrystals without precursor injection. Nanoscale Res Lett 2008, 3:213.CrossRef 28. Chen S, Bomer JG, Carlen

ET, Berg AV: Al 2 O 3 /silicon nanoISFET with near ideal Nernstian response. Nano Lett 2011, 11:2334.CrossRef 29. Asami H,

Abe https://www.selleckchem.com/products/fg-4592.html Y, Ohtsu T, Kamiya I, Hara M: Surface state analysis of photobrightening in CdSe nanocrystal thin films. J Phys Chem B 2003, 107:12566.CrossRef 30. Cuddy MF, Poda AR, Brantley LN: Determination of isoelectric points and the role of pH for common quartz crystal microbalance sensors. ACS Appl Mater Interfaces 2013, 5:3514.CrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions GS-1101 molecular weight PK fabricated and analyzed the EIS sensors. AP helped to fabricate these sensors also. TCT did XPS characteristics and analysis. This research work was carried out under the instruction of SM. First draft of this manuscript was written by PK. All of the authors revised the manuscript and approved it for publication.”
“Background

Macrophage plays an important role in the destabilization of atherosclerotic lesions. Molecular imaging approaches that target and image macrophages may be potentially useful towards predicting plaque vulnerability during the natural history of the disease [1–5]. Macrophages are effective efferocytes with the ability to recognize the externalized phosphatidylserine (PS) on the plasma membrane surface of apoptotic cells via the scavenger receptors and remove them from circulation and the arterial wall [6–9]. Phosphatidylserine is a naturally occurring phospholipid (PL) and its use for targeting macrophages may improve the biocompatibility of the contrast agent and avoid the use of exogenous targeting agents such as antibodies Benzatropine and peptides. This approach of using phosphatidylserine for targeting macrophages has been reported previously for magnetic resonance imaging of macrophage contents in atheroma with gadolinium-containing liposomes [10] but PS-containing micelles have not been reported. Lipid-polyethylene glycol (PEG) micelles have traditionally been used to solubilize hydrophobic drugs and solubilize hydrophobic nanoparticles into discrete clusters that can include either single or multiple nanoparticles in their cores and thus can achieve size tunability for particular application [11].

Diagn Microbiol Infect Dis 1999, 33:283–297.PubMedCrossRef 10. Choi S-H, Chung J-W, Lee E-J, et al.: Incidence, characteristics, and outcomes of Staphylococcus buy Z-VAD-FMK lugdunensis bacteremia. J Clin Microbiol 2010, 48:3346–3349.PubMedCrossRef 11. Fadel HJ,

Patel R, Vetter EA, Baddour LM: Clinical Significance of a Single Staphylococcus lugdunensis-Positive Blood Culture. J Clin Microbiol 2011, 49:1697–1699.PubMedCrossRef 12. Kawamura Y, Hou X-G, Sultana F, et al.: Distribution of Staphylococcus species among human clinical specimens and emended description of Staphylococcus caprae. J Clin Microbiol 1998, 36:2038–2042.PubMed 13. Shin JH, Jung HJ, Lee HR, Kim JH, Kim HR, Lee JN: Prevalence, identification, and antimicrobial susceptibility of Staphylococcus lugdunensis from various clinical specimens in Korea. Jpn J Infect Dis 2007, 60:312.PubMed 14. Kleeman KT, Bannerman

TL, Kloos WE: Species distribution of coagulase-negative staphylococcal isolates at a community hospital and implications for selection of staphylococcal identification procedures. Clin Microbiol 1993, 31:1318–1321. 15. De Paulis AN, Predari SC, Chazarreta CD, Santoianni JE: Five-test simple scheme for species-level identification of clinically significant coagulase-negative GSK-3 inhibition Staphylococci. J Clin Microbiol 2003, 41:1219–1224.PubMedCrossRef 16. Gatermann SG, GNAT2 Koschinski T, Friedrich S: Distribution and expression of macrolide resistance genes in coagulase-negative staphylococci. Clin Microbiol Infect 2007, 13:777–781.PubMedCrossRef 17. Frank KL, del Pozo JL, Patel R: From clinical microbiology to infection pathogenesis: How daring to be different works for Staphylococcus lugdunensis. Clin Microbiol Rev 2008, 21:111–133.PubMedCrossRef 18. Tan TY, Ng SY,

He J: Microbiological characteristics, presumptive identification, and antibiotic susceptibilities of Staphylococcus lugdunensis. J Clin Microbiol 2008, 46:2393–2395.PubMedCrossRef 19. Ghebremedhin B, Layer F, König W, König B: Genetic classification and distinguishing of Staphylococcus species based on different partial gap, 16 S rRNA, hsp60, rpoB, sodA, and tuf gene sequences. J Clin Microbiol 2008, 46:1019–1025.PubMedCrossRef 20. Piette A, Verschraegen G: Role of coagulase-negative staphylococci in human disease. Vet Microbiol 2009, 134:45–54.PubMedCrossRef 21. Hellbacher C, Törnqvist E, Söderquist B: Staphylococcus lugdunensis: clinical spectrum, antibiotic susceptibility, and phenotypic and genotypic patterns of 39 isolates. Clin Microbiol Infec 2006, 12:43–49.CrossRef 22. van der Mee-Marquet N, Achard A, Mereghetti L, Danton A, Minier M, Quentin R: Staphylococcus lugdunensis infections: high frequency of inguinal area carriage. J Clin Microbiol 2003, 41:1404–1409.PubMedCrossRef 23.

[29]. Nevertheless, comparison of the results of body mass obtained during the measurement 2, in 6 of 7 competitors suggested the necessity of reduction of BM2 from 1 to 6.6 kg (from 1.0% to 9.9%, the mean 4.7±3.0%) in order to meet the requirements of weight category limits. Reducing weight of some judokas during

training period was part of a training procedure, however, not all of the contestants, who participated in the study, was qualified for competition. The judoists, whose weight was above weight category limits, INK-128 had still 5 days before the beginning of the contest, which is typical time for rapid weight loss of weight-cyclers [30]. Since the fights are carried out within weight categories, body mass control is incorporated in judoists’ training regimes PCI32765 [31], but it does not necessarily have an impact on the reduction in motor abilities because the reduction in BM does not exceed 5% [32]. Kubo et al. [24] suggested that because of the division into the weight categories, the contestants with lower PF should reach higher sport skill level. However, no unequivocal results from studies in this field have been presented so far in the available literature [28]. From the physiological point of view, anaerobic power

and capacity, strength, and aerobic power have been considered the main characteristics to be developed by judo players [24, 28]. Anaerobic capacity is critical to the effectiveness of techniques used in attack and defense. According to Franchini et al. [33] the anaerobic system provides the short, quick, all-out bursts of maximal power during the match, while the aerobic system contributes to the athlete’s ability to sustain effort for the duration of the combat and to recover during the brief periods of rest or reduced effort. Therefore, Etoposide purchase we observed the post-training changes in the indices, with the most particular development being the time to obtaining peak power (toPP). Contrary to the

placebo group, judo contestants who were supplemented with creatine malate for 6 weeks had significantly higher values of the fatigue index (FI). These results were a natural consequence of faster depletion of muscle phosphagen stores (ATP and CP), mainly in skeletal muscles of type II, caused by generating higher peak power. However, the supplementation with creatine compounds showed no effect on aerobic capacity (VO2max), which was consistent with the observations by [4, 34]. In the study carried out among track and field athletes, mainly sprinters and long distance runners, these authors did not find significant changes in aerobic capacity after the supplementation with creatine malate.A significant increase, however, was found only in sprinters in peak power (PP and RPP) and total work (TW and RTW).

Figure 8 In vitro hydrolysis of DNA and RNA by Carocin S2. (A) Analysis of the DNase activity

of carocin S2. Lane M, the HindIII-digested λ DNA marker; lane 1, genomic DNA only; lanes 2 and 3, genomic DNA treated or untreated with carocin S2 in buffer, respectively; lane 4, equal quantity of EcoRI-digested genomic DNA. The 5′-labeled total RNA (B) and 3′-labeled total RNA (C) (1 μg of RNA per sample) were Trichostatin A cost incubated without (lane 1) or with 1 μg (lane 2), 100 ng (lane 3), 10 ng (lane 4), or 1 ng (lane 5) of Carocin S2 and the result was assessed by autoradiography. The arrowhead indicates that the RNA segment digested from ribosome. Equal amounts of Carocin S2I and Carocin S2K mixed before RNA digestion (lane 6). Surprisingly the RNA segments were larger when the RNA was Rucaparib manufacturer 3′-32P-labeled compared with 5′-32P-labeling (Figures 8B and 8C). As the concentrations of 23S RNA and 16S RNA decrease on the addition of increasing concentrations of CaroS2K, it is assumed that more ribosomal RNA is degraded leaving material

that is ostensibly the ribosome. When excess concentrations of caroS2K (i.e 1 μg) are added then most of the ribosomal RNA is degraded leading to a destabilization and subsequent degradation of the ribosome (Figure 8C, lane 2). We hence consider that CaroS2K (in sufficient amount) would degrade the ribosome. CaroS2I inhibits the killing activity of CaroS2K because a mixture of equal quantities of CaroS2K and CaroS2I prevented digestion of RNA segments by

CaroS2K (Figure 8C, lane 6). Subsequently, treatment of the genomic DNA of the indicator strain SP33 with the purified CaroS2K protein had no effect on deoxyribonuclease activity, as compared to the pattern of EcoRI-digested genomic Selleckchem Venetoclax DNA (Figure 8A and Additional file 1, Figure S4). Nucleotide sequence accession number The Genbank accession number of the sequence of the carocin S2 gene is HM475143. Discussion In this study, a chromosome-borne gene encoding bacteriocin, carocin S2, in Pcc strain 3F3 was shown to possess ribonuclease activity. According to Bradley’s classification, Carocin S2 is a low-molecular-weight bacteriocin [25]. Two genes, caroS2K and caroS2I, encode the 85-kDa and 10-kDa components, respectively, of Carocin S2. The substrate and gene structure of carocin S2 were unlike those of other bacteriocins from Pcc. On the basis of sequence analysis, carocin S2 comprises these two overlapping ORFs, caroS2K and caroS2I (Additional file 1, Figure S7). A putative Shine-Dalgarno sequence 5′-AUGGA-3′, which has also been seen in the DNA sequence of carocin S1, is located upstream (-9 bp to -13 bp) of the start codon AUG, suggesting that it could be a ribosome binding site for caroS2K [23].

The calculated IC50 value in this cell line for compound 2 is greater than 50 μM, for compound 5 it is 9.7 μM

and for compound 6 it is 9.1 μM. (B) Sensitivity of urothelial cancer cell lines and one representative normal uroepithelial control to compound 5 and compound 6 after 72 h of treatment. Y-27632 chemical structure The IC50 of compound 2 was only reached at concentrations near 50 μM. The cell lines outlined by bold letters were used for the functional experiments. While c5 and c6 significantly reduced the viability of all UCCs, their effect varied among the cell lines. It is noticeable that cells with an epithelial phenotype e.g. RT-112 were more sensitive than cells with a mesenchymal phenotype (SW-1710 and UM-UC-3; Figure 5B). The influence of the inhibitors on clonogenic growth after a 72 h treatment at the determined IC50 concentrations is illustrated in Figure 6. Compound 2

inhibited clonogenicity only in VM-CUB1 cells. Treatment with compound 5 resulted in a moderate reduction of colony numbers in RT-112, UM-UC-3 and 639-V cells, whereas in VM-CUB1 cells, clonogenic growth was completely abolished. In contrast, c5 had no effect on SW-1710 cells. Compound 6 was active in all cell lines, being most efficient in VM-CUB1, UM-UC-3 and 639-V cells. Figure 6 Effect of HDAC8 specific Raf phosphorylation inhibitor treatment on clonogenic growth of urothelial cancer cells. Giemsa-staining of grown colonies from

Acyl CoA dehydrogenase inhibitor treated RT-112, VM-CUB1, SW-1710, 639-V and UM-UC-3 cells is compared to DMSO solvent control (compound 2, compound 5, compound 6; IC50, 72 h). As the effect of pharmacological HDAC8 inhibition was stronger than the effect of HDAC8 knock-down, wound healing assays of UCCs after HDAC8 inhibitor treatment were additionally performed (Figure 7A). A clear difference was observed in VM-CUB1 and UM-UC-3 cells, respectively, comparing DMSO controls to cells treated with c5 and c6, especially after 6 – 12 h (Figure 7B). Figure 7 Migration assay of urothelial cancer cells after HDAC8 inhibitor treatment. (A) Representative photographs of wound healing assay at 0 and 12 hours from inhibitor treated RT-112, VM-CUB1, SW-1710, 639-V and UM-UC-3 cells (compound 2, compound 5, compound 6; IC50, 72 h) in comparison to a DMSO solvent control (co). (B) Relative scratch size after 3, 6, 9 and 12 h of migration in comparison to the starting point 0 h. The relative scratch size is displayed on the y-axis. p < 0.05 was regarded as significant and marked as *, whereas p < 0.01 and p < 0.001 were defined as highly significant and marked as ** and ***. The calculated significances refer to the DMSO solvent control. The impact of the HDAC8 inhibitor treatment was further analyzed by western blot analysis of different target proteins (Figure 8).

Increased expression of GCN2 coupled with decreased expression of CIMG_08909, a sky1p ortholog involved in mRNA splicing [40], is consistent with the hypothesis that the rate of protein production in day 2 spherules is lower than in mycelia Additional file 2: Table S3 lists the functional classification of all of the 184 C. immitis protein kinases and their S. cerevisiae homologs. 126 of these are eukaryotic protein kinases (ePKs) and

58 are atypical protein kinases (aPK). Of the ePK there are 47 novel kinases: 17 SRPKLs (serine/arginine rich protein kinase-like), 6 PezKs (pezizomycotina kinases) and 24 unclassified kinases designated as ‘Other’. We believe these 47 kinases to be novel because we did not observe orthologs in the species used for comparison, and they do not match families in kinase.com. There are 38 aPKs from well-known families, and 20 FunK1s (fungal kinase CH5424802 research buy 1s) from a family recently described in Coprinopsis cinerea[41] and Paracoccidioides[42].

Examining the classification of the differentially expressed protein kinases in day 2 spherules we found that 50% of STE11 kinases, 40% of the STE20 kinases and none of the STE7 kinases were downregulated compared to mycelia. 40% of the this website CAMK/CAMKL kinases are downregulated. Although the numbers are small, most of the protein kinases in the other/WEE, other/RAN and other/NAK classifications were downregulated. Table 2 Modulated protein kinases in day 2 and day 8 spherules Gene ID FCa FCb C. immitisannotation Classification gene S. cerevisiae CIMG_05093 −7.84 buy 5-FU 2.78 Serine/threonine-protein kinase; meiosis induction protein kinase CMGC/RCK/MAK IME2 * CIMG_09053 −6.68 6.18 Kinase domain containing protein CAMK/NNK1 NNK1 CIMG_07296 −5.60 5.26 Protein kinase domain containing protein CAMK/CAMKL/MARK YPL150W CIMG_01236 −5.46 — PAK kinase STE/STE20/PAKA STE20 * CIMG_00940 −5.28 — Protein kinase Other/WEE/SWE1 SWE1 ** CIMG_07521 −4.67 2.94 Protein kinase

domain containing protein; serine/threonine protein kinase 24 STE/STE20/YSK SPS1 * CIMG_04027 −4.65 3.81 serine/threonine protein kinase ssp1 Other/CAMKK None CIMG_03267 −4.55 — serine/threonine protein kinase CAMK/CAMKL/Kin4 KIN4 ** CIMG_07588 −4.52 — Kinase domain containing protein; checkpoint kinase Other/TTK MPS1 ** CIMG_01204 −4.34 4.02 protein kinase AGC/YANK None CIMG_08909 −4.14 3.06 Protein kinase, sky 1 CMGC/SRPK SKY1 CIMG_03947 −4.04 3.64 serine/threonine protein kinase CAMK/CAMKL/PASK PSK1 CIMG_03602 −3.98 3.70 Ran1-like protein kinase Other/RAN/VHS1 VHS1 ** CIMG_04103 −3.97 — cytokenesis protein sepH STE/STE11/CDC15 CDC15 ** CIMG_08220 −3.96 6.13 serine/threonine protein kinase ATG1 Other/ULK/ULK ATG1 CIMG_06932 −3.81 2.58 MAP kinase kinase kinase SskB STE/STE11/MEKK4 SSK2 CIMG_13010 −3.74 3.93 serine/threonine protein kinase Other/RAN/KSP1 KSP1 * CIMG_09191 −3.52 2.50 Protein kinase Other/HAL/HRK1 HRK1 CIMG_09469 −3.36 — Kinase domain containing protein Other/PEK None CIMG_03857 −3.

This latter suggests that the adaptive immune response developed towards biofilm bacteria during colonization would have restricted utility during invasive disseminated disease. Our studies also identify PsrP as one possible antigen

that may confer protection against both colonization and invasive disease. The other proteins identified as enhanced during biofilm formation and immunogenic during invasive disease may also represent novel targets for intervention. Methods All animal experiments www.selleckchem.com/screening/selective-library.html were reviewed and approved by the Institutional Animal Care and Use Committee at The University of Texas Health Science Center at San Antonio under protocol number 09022x-34. Strain and bacterial growth conditions Streptococcus pneumoniae strain TIGR4 is a serotype 4 clinical isolate whose genome has been sequenced and annotated

[44]. A66.1 is a serotype PLX4032 3 isolate that has also been previously described [24]. For planktonic growth, Todd Hewitt Broth (THB) was inoculated with overnight plate cultures and grown to mid-logarithmic phase (OD620 = 0.5; ~1.0 × 108 CFU/ml) at 37°C in 5% CO2. Mature biofilms were grown under once-through flow conditions as previously described [14]. Briefly, planktonic seed cultures were used to inoculate 1 meter long silicone tubing (0.89 mm internal diameter, Cole Parmer Inc., Vernon Hills, IL). Bacteria in the line were allowed to attach for 2 hours, after which the flow rate of THB was

adjusted to 0.035 ml/minute. Biofilm derived bacteria were harvested after 3 days by pinching the tube along its entire length, thereby removing the bacterial cells. One and two-dimensional gel electrophoresis and differential protein analysis For one-dimensional (1DGE) comparative analysis of proteins, whole cell lysates (25 μg) from the biofilm and planktonic pneumococci were separated by 12% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and silver stained using standard methods. Two-dimensional electrophoresis (2DGE) was conducted according to the principles of O’Farrell [45], and done using the optimized conditions for S. pneumoniae as previously described by Allegrucci et al. [24]. Briefly, planktonic and biofilm pneumococci were collected, washed, and suspended in TE buffer (10 mM Tris-HCl, 1 Carnitine palmitoyltransferase II mM EDTA, pH 8.0) supplemented with 300 μg/ml phenylmethyslfonylfluoride (Sigma, St. Louis, MO). Bacteria were disrupted by sonication on ice using 6, 10-second bursts. Samples were prepared for isoelectric focusing (IEF) using a ReadyPrep 2-D cleanup kit (Bio-Rad, Hercules, CA) after which the protein pellet was dissolved in DeStreak rehydration solution (GE Healthcare, Piscataway, NJ). Protein levels were quantified using a Non-Interfering protein assay (G-Biosciences, Maryland Heights, MO). For each sample, 300 μg of protein were applied to 11-cm Immobiline DryStrips (pH 3-5.

1, JN119854.1, JN108899.1, HQ880271.1, GU944731.1, GU120473.1, JQ780837.1 and HQ880255.1) and 5 clinical strains (Table 2, including 3 strains of Klebsiella pneumoniae and 2 strains of Escherichia coli) were selected as positive controls, Escherichia

coli ATCC#25922 and Escherichia coli J53 were used as negative controls. In the initial experiment, the distributions of aminoglycoside resistance genes among those controls strains were confirmed by conventional PCR with the specific primers listed in Table 3. Fifty six clinical isolates of Enterobacteriaceae were used to evaluate the utility of GeXP assay. All the clinical samples were taken as part of standard patient care from the inpatients at Guangzhou First Municipal People’s Hospital from January learn more 2008 to December 2009. This protocol was approved by the Committee on the Use of Human Subjects in Research at Guangzhou First Municipal People’s Hospital, an affiliated hospital of Guangzhou Medical College. All the informed consents from the inpatients themselves or their guardians were obtained. In initial experiments, the identification of the clinical isolates and the minimum inhibitory concentrations (MICs) of antibiotics www.selleckchem.com/products/Adrucil(Fluorouracil).html were confirmed

by the VITEK® 2 system (bioMérieux, France) (Additional file 1). Forty eight of the 56 isolates (including 30 strains of Klebsiella pneumoniae and 18 strains of Escherichia coli) presented resistance to gentamicin (MIC≥16μg/mL), tobramycin (MIC≥16μg/mL) and/or amikacin (MIC≥64μg/mL), the other 8 isolates (including 5 strains of Klebsiella pneumoniae Tangeritin and 3 strains of Escherichia coli) were susceptible to gentamicin (MIC≤4μg/mL), tobramycin (MIC≤4μg/mL) and amikacin (MIC≤16μg/mL) according to the standards of Clinical and Laboratory Standards Institute (CLSI 2012). Table 1 Distribution of aminoglycoside resistance genes in 8

reference strains Strains No. Reference strains Presence of aminoglycoside resistance genes GenBank accession no. NF512663 Escherichia coli aac(6’)-Ib [aacA4]* JN108884.1 NF802568 Escherichia coli ant(3”)-II [aadA2] * JN119854.1 NF811738 Klebsiella pneumoniae aac(6’)-Ib [aacA4] *& ant(3”)-I [aadA1] * JN108899.1 NF707346 Klebsiella pneumoniae ant(2”)-I [aadB] *& ant(3”)-I [aadA1] * HQ880271.1 NF802824 Klebsiella pneumoniae acc(6’)-II GU944731.1 NF811834 Klebsiella pneumoniae aadA5 GU120473.1 NF141160 Acinetobacter baumannii aac(3’)-I [aacC1] * & ant(3”)-I [aadA1] * JQ780837.1 NF910192 Pseudomonas putida aac(6’)-II & ant(2”)-I [aadB] * HQ880255.1 * Synonyms in the bracket. Table 2 Distribution of aminoglycoside resistance genes in 5 positive control isolates Strains No.

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