Evaluation of a modified double-disc synergy test for detection of extended spectrum β-lactamases in AMPC β-lactamase-producing proteus mirabilis

The detection of extended-spectrum β-lactamases (ESBLs) in gram-negative bacteria that produce AmpC β-lactamases is problematic. In the present study, the performance of modified double-disc synergy test (MDDST) that employs a combination of cefepime and piperacillin-tazobactam for the detection of proteus mirabilis producing extended spectrum and AmpC β-lactamases was evaluated and compared with double-disc synergy test (DDST) and NCCLS phenotypic disc confirmatory test (NCCLS-PDCT). A total of 90 clinical isolates of P. mirabilis , which met the CLSI (Clinical and Laboratory Standards Institute) screening criteria that these had broth microdilution (BMD) MIC of ≥2 mg/mL for at least one extended spectrum cephalosporin [ceftazidime (CAZ), cefotaxime (CTX) and cefpodoxime], were selected for the study. MDDST detected ESBLs in 40/90 of the isolates, whereas DDST detected ESBLs in only 25 isolates. NCCLS-PDCT could detect ESBLs in 39 isolates using CAZ and CAZ + clavulanic acid (CLA) combination, whereas CTX and CTX + CLA combination could detect only 37 isolates as ESBL positive. As many as 34/40 ESBL positive isolates were confirmed to be AmpC β-lactamase positive by the modified three-dimensional test (MTDT). MDDST and NCCLS-PDCT could detect ESBLs in all the 34 AmpC positive isolates, whereas DDST could detect ESBLs in only 19 isolates. The study demonstrated that MDDST is superior to DDST and as sensitive as NCCLS-PDCT. However, MDDST seems to have enhanced potential for the detection of ESBLs in AmpC β-lactamase-producing P. mirabilis

Effect of yttrium(Y) on structural, morphological and transport properties of CdO thin films prepared by spray pyrolysis technique

Cadmium oxide (CdO) and yttrium (Y) doped CdO (Y: CdO) thin films have been prepared onto glass substrate at temperature 300 °C by spray pyrolysis technique. The effects of yttrium (Y) doping on the structural, morphology, optical and electrical properties were studied systematically. The X-ray diffraction (XRD) study confirms that CdO films are polycrystalline in nature with cubic structure having lattice parameter of 0.4658 nm. Surface topographic and nano-structural analysis indicates cluster grain size and porosity decreased substantially with increase of yttrium (Y) content in CdO films. The optical transmittance exhibits excellent optical transparency, with an average transmittance of >70% in the visible range for 2 to 4% yttrium (Y) doping. The optical band gap widens in Y: CdO film from 2.24 to 2.62 eV through Burstein- Moss shift. Hall measurement confirms that material is of n type with a minimum resistivity of 4.7 × 10−4 Ω-cm with carrier concentration of 4.2 × 1021 cm−3 were achieved for 2% yttrium (Y) doping

Heat and PAHs emissions in indoor kitchen air and its impact on kidney dysfunctions among kitchen workers in Lucknow, North India

10.1371/journal.pone.0148641PLoS ONE112e014864

alpha,beta-Unsaturated Carbonyl System of Chalcone-Based Derivatives Is Responsible for Broad Inhibition of Proteasomal Activity and Preferential Killing of Human Papilloma Virus (HPV) Positive Cervical Cancer Cells

Proteasome inhibitors have potential for the treatment of cervical cancer. We describe the synthesis and biological characterization of a new series of 1,3-diphenylpropen-1-one (chalcone) based derivatives lacking the boronic acid moieties of the previously reported chalcone-based proteasome inhibitor 3,5-bis(4-boronic acid benzylidene)-1-methylpiperidin-4-one and bearing a variety of amino acid substitutions on the amino group of the 4-piperidone. Our lead compound 2 (RA-1) inhibits proteasomal activity and has improved dose-dependent antiproliferative and proapoptotic properties in cervical cancer cells containing human papillomavirus. Further, it induces synergistic killing of cervical cancer cell lines when tested in combination with an FDA approved proteasome inhibitor. Exploration of the potential mechanism of proteasomal inhibition by our lead compound using in silico docking studies suggests that the carbonyl group of its oxopiperidine moiety is susceptible to nucleophilic attack by the gamma-hydroxythreonine side chain within the catalytic sites of the proteasome