Reinvestigation of the tautomerism of some substituted 2-hydroxypyridines

n/

Could SARS-CoV-2 Have Bacteriophage Behavior or Induce the Activity of Other Bacteriophages?

SARS-CoV-2 has become one of the most studied viruses of the last century. It was assumed that the only possible host for these types of viruses was mammalian eukaryotic cells. Our recent studies show that microorganisms in the human gastrointestinal tract affect the severity of COVID-19 and for the first time provide indications that the virus might replicate in gut bacteria. In order to further support these findings, in the present work, cultures of bacteria from the human microbiome and SARS-CoV-2 were analyzed by electron and fluorescence microscopy. The images presented in this article, in association with the nitrogen (15N) isotope-labeled culture medium experiment, suggest that SARS-CoV-2 could also infect bacteria in the gut microbiota, indicating that SARS-CoV-2 could act as a bacteriophage. Our results add new knowledge to the understanding of the mechanisms of SARS-CoV-2 infection and fill gaps in the study of the interactions between SARS-CoV-2 and non-mammalian cells. These findings could be useful in suggesting specific new pharmacological solutions to support the vaccination campaign

Effects of triclosan in the freshwater mussel Dreissena polymorpha: a proteomic investigation

Triclosan (TCS, 5-chloro-2-(2,4-dichlorophenoxy)phenol) is commonly used in several personal care products, textiles, and children's toys. Because the removal of TCS by wastewater treatment plants is incomplete, its environmental fate is to be discharged into freshwater ecosystems, where its ecotoxicological impact is still largely unexplored. Previously, we began a structured multi-tiered approach in order to evaluate TCS toxicity in the freshwater mussel Dreissena polymorpha. The results of our previous studies, based on in vitro and in vivo experiments, highlighted a pronounced cytogenotoxic effect exerted by TCS, and showed that an increase in oxidative stress was likely to be one of its main toxic mechanisms. In this work, in order to investigate TCS toxicity mechanisms in aquatic non-target species in greater depth, we decided to use a proteomic approach, analysing changes in protein expression profiles in gills of D. polymorpha exposed for seven days to TCS. Moreover, thiobarbituric acid reactive substances (TBARS) were measured to investigate further the role played by TCS in inducing oxidative stress. Finally, TCS bioaccumulation in mussel tissues was also assessed, to ensure an effective accumulation of the toxicant. Our results not only confirmed the role played by TCS in inducing oxidative stress, but furthered knowledge about the mechanism exerted by TCS in inducing toxicity in an aquatic non-target organisms. TCS induced significant alterations in protein expression profiles in gills of D. polymorpha. The wide range of proteins affected suggested that this chemical has marked effects on various biological processes, especially those involved in calcium binding or stress response. We also confirmed that the proteomic analysis, using 2-DE and de novo sequencing, is a reliable and powerful approach to investigate cellular responses to pollutants in a non-model organism with few genomic sequences available in databases

A redox proteomic investigation of oxidative stress caused by benzoylecgonine in the freshwater bivalve Dreissena polymorpha

Drugs of abuse and their human metabolites have been recently recognized as emerging environmental contaminants. Notwithstanding the fact that these kinds of compounds share some features with pharmaceuticals, their ecotoxicology has not yet been extensively investigated, although some of their characteristics may potentially threaten aquatic ecosystems. One of the most abundant drugs found in rivers and wastewaters is benzoylecgonine (BE), the main metabolite of cocaine. We applied a redox proteomics approach to evaluate changes in the proteome of Dreissena polymorpha exposed to two different concentrations of BE (0.5 and 1 mu g/l). Exposures were performed in vivo for a period of 14days and the effect of oxidative stress on protein thiol and carbonyl groups in mussel gills were evaluated. One-dimensional electrophoresis did not reveal a reduction in protein thiol content but showed a significant increase of protein carbonylation at both doses tested. Then, protein profiling using two-dimensional gel electrophoresis was performed with subsequent matrix assisted laser desorption/ionization time-of-flight (MALDI-TOF) and TOF/TOF with LIFT technique and linear ion trap combined with orbitrap mass spectrometer (LTQ-Orbitrap). This yielded de novo protein sequences suitable for database searching. These preliminary results and protein identifications obtained suggest that BE causes oxidative stress. Oxidative modifications were detected in differing classes of proteins such as those of the cytoskeleton, energetic metabolism and stress response