Characterization of zinc oxide nanocrystals with different morphology for application in ultraviolet‐light photocatalytic performances on rhodamine B

ZnO nanostructures of different morphology (nanorods, nano‐leaf, nanotubes) were favourably grown using a chemical precipitation process. The prepared ZnO nanostructures were characterized systematically using absorption spectroscopy, emission spectroscopy, X‐ray diffraction (XRD), scanning electron microscopy (SEM) and Fourier transform infrared studies. XRD results showed the hexagonal wurtzite phase of the synthesized ZnO nanostructures. Structural properties such as average crystallite size, lattice constants, volume of the unit cell, atomic fraction, and structural bonds were also studied. The optical band gap of the synthesized ZnO nanocrystals varied from 3.52 eV to 3.69 eV with high quantum yield of the blue emission (~420 nm). Urbach energy for ZnO nanocrystals was calculated to be 0.702 eV, 0.901 eV, and 0.993 eV for nanorods, nano‐leaf, and tube like ZnO crystals, respectively. Morphology of the fabricated nanostructures was investigated using SEM. Photocatalytic degradation of rhodamine B (Rh B) in solution under UV irradiation was explored with different ZnO morphology. Photocatalytic experiments showed that ZnO nano‐leaf had a higher degradation rate of photocatalytic activity of photodegrading Rh B compared with the other tube shape and rods shape nanostructures. The Rh B dye degraded considerably by ～79.05%, 74.41%, and 69.8% within 120 min in the presence of the as‐fabricated fern nano‐leaf, nanotubes, and nanorods of the ZnO nanocrystals at room temperature.     

Loop-mediated isothermal amplification based identification of entomopathogenic nematodes Heterorhabditis spp. and Steinernema spp. from soil DNA

Entomopathogenic nematodes (EPNs) of the genera Heterorhabditis and Steinernema kill insects with the help of their symbiotic bacteria. They are widely used as biocontrol agents to manage insect pests of crops. The infective juveniles (IJ) of EPNs are isolated from soil by insect baiting technique, which is labour-intensive, time-consuming, wasteful, and inefficient. Here, we present loop-mediated isothermal amplification (LAMP) assays for rapid detection of Heterorhabditis spp. (Het-LAMP) and Steinernema spp. (Ste-LAMP) from total soil DNA. The primers for Het-LAMP and Ste-LAMP were designed using ITS and 18S rDNA regions of genomic DNA. The LAMP reactions could be completed in 60 min, at 66 °C and 68 °C, respectively, followed by termination at 85 °C for 5 min. The assays were highly sensitive and could detect up to 0.02 picograms of Heterorhabditis DNA and 96 picograms of Steinernema DNA in a 25 μl reaction. Both the assays were specific for the target nematode species and detected the presence of a single IJ in the total DNA extracted from 250 mg of soil. The assays developed in this study would be of immense utility for the efficient detection and identification of native EPNs in large-scale surveys. These assays are amenable to automation and could be used to develop convenient detection kits for point-of-service diagnosis of EPNs in the field without the need for a trained and experienced personnel.

     

In-Silico Proteomic Exploratory Quest: Crafting T-Cell Epitope Vaccine Against Whipple’s Disease

International Journal of Peptide Research and Therapeutics - Whipple’s disease is one of the rare maladies in terms of spread but very fatal one as it is linked with many disorders (like...     

Novel Neuroprotective Function of Apical-Basal Polarity Gene Crumbs in Amyloid Beta 42 (Aβ42) Mediated Neurodegeneration

Alzheimer''s disease (AD, OMIM: 104300), a progressive neurodegenerative disorder with no cure to date, is caused by the generation of amyloid-beta-42 (Aβ42) aggregates that trigger neuronal cell death by unknown mechanism(s). We have developed a transgenic Drosophila eye model where misexpression of human Aβ42 results in AD-like neuropathology in the neural retina. We have identified an apical-basal polarity gene crumbs (crb) as a genetic modifier of Aβ42-mediated-neuropathology. Misexpression of Aβ42 caused upregulation of Crb expression, whereas downregulation of Crb either by RNAi or null allele approach rescued the Aβ42-mediated-neurodegeneration. Co-expression of full length Crb with Aβ42 increased severity of Aβ42-mediated-neurodegeneration, due to three fold induction of cell death in comparison to the wild type. Higher Crb levels affect axonal targeting from the retina to the brain. The structure function analysis identified intracellular domain of Crb to be required for Aβ42-mediated-neurodegeneration. We demonstrate a novel neuroprotective role of Crb in Aβ42-mediated-neurodegeneration.     

Altered Antibody Profiles against Common Infectious Agents in Chronic Disease

Despite the important diagnostic value of evaluating antibody responses to individual human pathogens, antibody profiles against multiple infectious agents have not been used to explore health and disease mainly for technical reasons.  We hypothesized that the interplay between infection and chronic disease might be revealed by profiling antibodies against multiple agents. Here, the levels of antibodies against a panel of 13 common infectious agents were evaluated with the quantitative Luciferase Immunoprecipitation Systems (LIPS) in patients from three disease cohorts including those with pathogenic anti-interferon-γ autoantibodies (IFN-γ AAB), HIV and Sjögren’s syndrome (SjS) to determine if their antibody profiles differed from control subjects.  The IFN-γ AAB patients compared to controls demonstrated statistically higher levels of antibodies against VZV (p=0.0003), EBV (p=0.002), CMV (p=0.003), and C. albicans (p=0.03), but lower antibody levels against poliovirus (p=0.04). Comparison of HIV patients with blood donor controls revealed that the patients had higher levels of antibodies against CMV (p=0.0008), HSV-2 (p=0.0008), EBV (p=0.001), and C. albicans (p=0.01), but showed decreased levels of antibodies against coxsackievirus B4 (p=0.0008), poliovirus (p=0.0005),   and HHV-6B (p=0.002). Lastly, SjS patients had higher levels of anti-EBV antibodies (p=0.03), but lower antibody levels against several enteroviruses including a newly identified picornavirus, HCoSV-A (p=0.004), coxsackievirus B4 (p=0.04), and poliovirus (p=0.02). For the IFN-γ AAB and HIV cohorts, principal component analysis revealed unique antibody clusters that showed the potential to discriminate patients from controls.  The results suggest that antibody profiles against these and likely other common infectious agents may yield insight into the interplay between exposure to infectious agents, dysbiosis, adaptive immunity and disease activity.     

Rapid Identification of Sequences for Orphan Enzymes to Power Accurate Protein Annotation

The power of genome sequencing depends on the ability to understand what those genes and their proteins products actually do. The automated methods used to assign functions to putative proteins in newly sequenced organisms are limited by the size of our library of proteins with both known function and sequence. Unfortunately this library grows slowly, lagging well behind the rapid increase in novel protein sequences produced by modern genome sequencing methods. One potential source for rapidly expanding this functional library is the “back catalog” of enzymology – “orphan enzymes,” those enzymes that have been characterized and yet lack any associated sequence. There are hundreds of orphan enzymes in the Enzyme Commission (EC) database alone. In this study, we demonstrate how this orphan enzyme “back catalog” is a fertile source for rapidly advancing the state of protein annotation. Starting from three orphan enzyme samples, we applied mass-spectrometry based analysis and computational methods (including sequence similarity networks, sequence and structural alignments, and operon context analysis) to rapidly identify the specific sequence for each orphan while avoiding the most time- and labor-intensive aspects of typical sequence identifications. We then used these three new sequences to more accurately predict the catalytic function of 385 previously uncharacterized or misannotated proteins. We expect that this kind of rapid sequence identification could be efficiently applied on a larger scale to make enzymology’s “back catalog” another powerful tool to drive accurate genome annotation.