Publications by authors named "Teresa Lopizzo"
Article Synopsis
- A multi-center study in Southern Italy evaluated the resistance of clinical isolates from bloodstream infections, pneumonia, and urinary tract infections to the β-lactam-β-lactamase inhibitor ceftazidime-avibactam (CZA), noting an 81.7% susceptibility rate.
- Among the resistance mechanisms identified, metallo-β-lactamases were predominant, particularly VIM-type, and resistance was linked to specific high-risk clones like ST111 and ST235.
- The study emphasizes the need for effective surveillance systems to monitor and control resistance development and the spread of high-risk bacterial clones.
Dipeptidyl amino-peptidase 3 (DPP3) is an aminopeptidase that is released into circulation upon cell death. DPP3 is involved in the degradation of angiotensins, enkephalines, and endomorphines. It has been shown that circulating DPP3 (cDPP3) plasma concentration increases in cardiogenic shock (CS) patients and correlates with high mortality risk.
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- Carbapenemase-producing Enterobacterales (CPE) pose a serious health threat due to their resistance to most antibiotics, with ceftazidime/avibactam (CAZ/AVI) recently approved for treating infections caused by these bacteria.
- A study conducted during the first wave of the COVID-19 pandemic in southern Italy evaluated the prevalence of CAZ/AVI resistance among carbapenem-resistant K. pneumoniae (CR-Kp) from bloodstream infections and hospital-acquired pneumonia.
- Out of 89 CR-Kp isolates sampled, 3 were found to be resistant to CAZ/AVI, with one being a KPC-type producer and others producing NDM and VIM variants, indicating that while
Biochemical characterization of the THIN-B metallo-beta-lactamase of Janthinobacterium lividum.
Antimicrob Agents Chemother
December 2004
The THIN-B metallo-beta-lactamase, a subclass B3 enzyme produced by the environmental species Janthinobacterium lividum, was overproduced in Escherichia coli by means of a T7-based expression system. The enzyme was purified (>95%) by two ion-exchange chromatography steps and subjected to biochemical analysis. The native THIN-B enzyme is a monomeric protein of 31 kDa.
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