Publications by authors named "M Malesevic"
Purpose: The present study investigated the role of resistance-nodulation-cell division (RND) efflux pumps in tigecycline resistance of Acinetobacter baumannii clinical isolates recovered from three Western Balkan countries (Serbia, Bosnia and Herzegovina and Montenegro).
Methods: A total of 37 A. baumannii isolates recovered from seven tertiary care hospitals in 2016 and 2022 were tested against tigecycline using broth microdilution method.
Article Synopsis
- The study aimed to evaluate the effects of electrolytic versus nonelectrolytic toothbrushing on periodontal health and bacteria in dogs.
- A total of 26 dogs participated, with one group using an electrolytic toothbrush and the other using a standard toothbrush, and both groups underwent oral examinations and bacterial sampling over an eight-week period.
- Results showed significant improvements in gum and calculus indices in the electrolytic group, while the control group experienced a worsening plaque index and increased levels of harmful bacteria.
SlyD is a widely-occurring prokaryotic FKBP-family prolyl isomerase with an additional chaperone domain. Often, such as in Escherichia coli, a third domain is found at its C-terminus that binds nickel and provides it for nickel-enzyme biogenesis. SlyD has been found to bind signal peptides of proteins that are translocated by the Tat pathway, a system for the transport of folded proteins across membranes.
View Article and Find Full Text PDFInfections caused by multidrug-resistant pathogens are one of the biggest challenges facing the healthcare system today. Quorum quenching (QQ) enzymes have the potential to be used as innovative enzyme-based antivirulence therapeutics to combat infections caused by multidrug-resistant pathogens. The main objective of this research was to describe the novel YtnP lactonase derived from the clinical isolate Stenotrophomonas maltophilia and to investigate its antivirulence potential against multidrug-resistant Pseudomonas aeruginosa MMA83.
View Article and Find Full Text PDFArticle Synopsis
- Systemic AA amyloidosis is a disease caused by the misfolding of serum amyloid A (SAA) protein, leading to harmful deposits in various organs.
- The study aimed to discover new substances that can inhibit the formation of amyloid fibrils from SAA protein and to understand how they work.
- Researchers identified lysozyme as an effective inhibitor of SAA fibril formation, which seems to function by directly binding to SAA and preventing its aggregation, similar to how molecular chaperones operate.