Zinc chloride is effective as an antibiotic in biofilm prevention following septoplasty.

Biofilm-state bacterial infections associated with inserted medical devices constitute a massive health and financial problem worldwide. Although bacteria exhibit significantly lower susceptibility to antibiotics in the biofilm state, the most common treatment approach still relies on antibiotics, exacerbating the phenomenon of antibiotic-resistant bacteria. In this study, we aimed to assess whether ZnCl2 coating of intranasal silicone splints (ISSs) can reduce the biofilm infections associated with the insertion of these devices and prevent the overuse of antibiotics while minimizing waste, pollution and costs. We tested the ability of ZnCl2 to prevent biofilm formation on ISS both in vitro and in vivo by using the microtiter dish biofilm formation assay, crystal violet staining, and electron and confocal microscopy. We found a significant decrease in biofilm formation between the treatment group and the growth control when ZnCl2-coated splints were placed in patients' nasal flora. According to these results, infections associated with ISS insertion may be prevented by using ZnCl2 coating, thereby obviating the overuse and abuse of antibiotics.

Modification of topoisomerase I activity by glucose and by O-GlcNAcylation of the enzyme protein.

The regulation of topoisomerase I (topo I) activity is of prime importance for gene expression. It participates in DNA replication, transcription, recombination, and DNA repair, and serves as a target for anticancer drugs. Many proteins and enzymes are modified by O-linked beta-N-acetylglucosamine (O-GlcNAc), which exerts profound effects on their function. However, the modification of topo I by O-GlcNAc and the effect on its activity has not been previously reported. Here, we show that topo I protein is modified by O-GlcNAc in vitro in the porcine proximal tubular epithelial cell line (LLPCK-1), and in vivo in the mouse kidney. The level of O-GlcNAcylation of topo I protein correlates well with the enzyme activity, namely, a decrease in O-GlcNAc results in a reduction in topo I activity, and vice versa. O-GlcNAc transferase (OGT) was coprecipitated with topo I protein, suggesting a possible interaction between both enzymes. In addition, treatment of cells with glucosamine increased topo I activity and O-GlcNAcylation. The results of this study provide a novel mechanism for the regulation of topo I activity. Topo I is important for DNA transcription, therefore, its regulation by GlcNAcylation contributes to the mechanism by which glucose levels affect gene expression, and may pave the way to the development of new drugs that could control topo I activity.