Quinolone resistance in bacterial pathogens has primarily been associated with mutations in the quinolone resistance-determining regions (QRDRs) of bacterial type-II topoisomerases, which are DNA gyrase and topoisomerase IV. Depending on the position and type of the mutation (s) in the QRDRs, bacteria either become partially or completely resistant to quinolone. QRDR mutations have been identified and characterized in Salmonella enterica isolates from around the globe, particularly during the last decade, and efforts have been made to understand the propensity of different serovars to carry such mutations. Because there is currently no thorough analysis of the available literature on QRDR mutations in different Salmonella serovars, this review aims to provide a comprehensive picture of the mutational diversity in QRDRs of Salmonella serovars, summarizing the literature related to both typhoidal and non-typhoidal Salmonella serovars with a special emphasis on recent findings. This review will also discuss plasmid-mediated quinolone-resistance determinants with respect to their additive or synergistic contributions with QRDR mutations in imparting elevated quinolone resistance. Finally, the review will assess the contribution of membrane transporter-mediated quinolone efflux to quinolone resistance in strains carrying QRDR mutations. This information should be helpful to guide the routine surveillance of foodborne Salmonella serovars, especially with respect to their spread across countries, as well as to improve laboratory diagnosis of quinolone-resistant Salmonella strains.

Proteases are widely used to remove affinity and solubility tags from recombinant proteins to avoid potential interference of these tags with the structure and function of the fusion partner. In recent years, great interest has been seen in use of the human rhinovirus 3C protease owing to its stringent sequence specificity and enhanced activity. Like other proteases, activity of the human rhinovirus 3C protease can be affected in part by the buffer components and additives that are generally employed for purification and stabilization of proteins, hence, necessitate their removal by tedious and time-consuming procedures before proteolysis can occur. To address this issue, we examined the effect of elution buffers used for common affinity based purifications, salt ions, stability/solubility and reducing agents, and detergents on the activity of the human rhinovirus 3C protease using three different fusion proteins at 4°C, a temperature of choice for purification of many proteins. The results show that the human rhinovirus 3C protease performs better at 4°C than the frequently used tobacco etch virus protease and its activity was insensitive to most of the experimental conditions tested. Though number of fusion proteins tested is limited, we expect that these finding will facilitate the use of the human rhinovirus 3C protease in recombinant protein production for pharmaceutical and biotechnological applications.

Acriflavine resistance protein B (AcrB) serves as prototype for multidrug resistance (MDR) efflux transporters of resistance nodulation division (RND) superfamily. AcrB has been proven as...

Excessive use of detergents in wide industrial processes results in unwanted surfactant pollution. Among them, sodium dodecyl sulphate (SDS) has well-known history to be used in pharmaceutical and industrial applications. However, if discharged without treatment, it can cause toxic effects on living organisms especially to the aquatic life. Floating treatment wetlands (FTWs) could be a cost-effective and eco-friendly options for the treatment of wastewater containing SDS. In this study, FTWs mesocosms were established in the presence of hydrocarbons-degrading bacteria. Two plant species (Brachiaria mutica and Leptochloa fusca) were vegetated and a consortium of bacteria (Acinetobacter sp. strain BRSI56, Acinetobacter junii strain TYRH47, and Acinetobacter sp. strain CYRH21) was applied to enhance degradation in a short-time. Results illustrated that FTWs vegetated with both plants successfully removed SDS from water, however, bacterial augmentation further enhanced the removal efficiency. Maximum reduction in SDS concentration (97.5%), chemical oxygen demand (92.0%), biological oxygen demand (94.2%), and turbidity (99.4%) was observed in the water having FTWs vegetated with B. mutica and inoculated with the bacteria. The inoculated bacteria showed more survival in the roots and shoots of B. mutica as compared to L. fusca. This study concludes that FTWs have the potential for the removal of SDS from contaminated water and their remediation efficiency can be enhanced by bacterial augmentation.