Adenoviruses are important human pathogens that have been developed as vectors for gene therapies and genetic vaccines. Previous studies indicated that human infections with adenoviruses are self-limiting in immunocompetent hosts with evidence of some persistence in adenoid tissue. We sought to better understand the natural history of adenovirus infections in various non-human primates and discovered that healthy populations of great apes (chimpanzees, bonobos, gorillas, and orangutans) and macaques shed substantial quantities of infectious adenoviruses in stool. Shedding in stools from asymptomatic humans was found to be much less frequent, comparable to frequencies reported before. We purified and fully sequenced 30 novel adenoviruses from apes and 3 novel adenoviruses from macaques. Analyses of the new ape adenovirus sequences (as well as the 4 chimpanzee adenovirus sequences we have previously reported) together with 22 complete adenovirus genomes available from GenBank revealed that (a) the ape adenoviruses could clearly be classified into species corresponding to human adenovirus species B, C, and E, (b) there was evidence for intraspecies recombination between adenoviruses, and (c) the high degree of phylogenetic relatedness of adenoviruses across their various primate hosts provided evidence for cross species transmission events to have occurred in the natural history of B and E viruses. The high degree of asymptomatic shedding of live adenovirus in non-human primates and evidence for zoonotic transmissions warrants caution for primate handling and housing. Furthermore, the presence of persistent and/or latent adenovirus infections in the gut should be considered in the design and interpretation of human and non-human primate studies with adenovirus vectors.
N-Terminally Fmoc protected amino acid, Fmoc-Phe-OH (Fmoc-L-Phenylalanine-OH), forms an efficient, stable and transparent hydrogel with a minimum gelation concentration of 0.1% w/v. This hydrogel has been nicely utilized to prepare and stabilize fluorescent few-atom silver nanoclusters. Interestingly, in absence of any toxic reducing agents in a water medium, silver ions are complexed with the carboxylate group of the Fmoc-Phe-OH gelator, and they are reduced spontaneously in the presence of diffused sunlight at physiological pH (7.46) and room temperature to form silver nanoclusters. The three dimensional structure provided by the hydrogel helps to stabilize newly formed silver nanoclusters within the hydrogel matrix. These clusters have been examined using UV-Vis, photoluminescence spectroscopy, high resolution transmission electron microscopy (HR-TEM), X-ray powder diffraction (XRPD) and matrix-assisted laser-desorption ionization (MALDI) mass spectrometric analysis. MALDI mass spectrometric analysis shows the presence of just a few atoms within the silver cluster as Ag 4 . These silver nanoclusters exhibit interesting fluorescent properties including large Stokes shift (more than 110 nm), narrow emission band width (36 AE 1 nm) and a quantum yield of 3.76%. These silver nanoclusters are stable for up to 4 months of storage at 4 C in the dark. The morphology of the hydrogel changes after the encapsulation of silver ions within the gel and this altered morphology is retained after the formation of silver nanoclusters within the gel. Interestingly, the rheological properties of the hydrogel alone are different from that of the silver nanocluster-containing hydrogel.
A new synthetic tripeptide-based hydrogel has been discovered at physiological pH and temperature. This hydrogel has been thoroughly characterized using different techniques including field emission scanning electron microscopic (FE-SEM) and high-resolution transmission electron microscopic (HR-TEM) imaging, small- and wide-angle X-ray diffraction analyses, FT-IR, circular dichroism, and rheometric analyses. Moreover, this gel exhibits thixotropy and injectability. This hydrogel has been used for entrapment and sustained release of an antibiotic vancomycin and vitamin B12 at physiological pH and temperature for about 2 days. Interestingly, MTT assay of these gelator molecules shows almost 100% cell viability of this peptide gelator, indicating its noncytotoxicity.
A long-chain amino acid containing dipeptide has been found to form a hydrogel in phosphate buffer whose pH ranges from 6.0 to 8.8. The hydrogel formed at pH 7.46 has been characterized by small-angle X-ray scattering (SAXS), wide-angle powder X-ray diffraction (PXRD), Fourier transform infrared (FT-IR) spectroscopy, field-emission scanning electron microscopy (FE-SEM), high-resolution transmission electron microscopy (HR-TEM) imaging and rheological analyses. The microscopic imaging studies suggest the formation of a nanofibrillar three-dimensional (3D) network for the hydrogel. As observed visually and confirmed rheologically, the hydrogel at pH 7.46 exhibits thixotropy. This thixotropic property can be exploited to inject the peptide. Furthermore, the hydrogel exhibits remarkable antibacterial activity against Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa, which are responsible for many common diseases. The hydrogel has practical applicability due to its biocompatibility with human red blood cells and human fibroblast cells. Interestingly, this hydrogel shows high resistance toward proteolytic enzymes, making it a new potential antimicrobial agent for future applications. It has also been observed that a small change in molecular structure of the gelator peptide not only turns the gelator into a nongelator molecule under similar conditions, but it also has a significant negative impact on its bactericidal character.
Mitochondria exert important control over plasma membrane (PM) Orai1 channels mediating store-operated Ca 2+ entry (SOCE).
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