Impact of COVID-19 on healthcare-associated infections and antimicrobial use in Italy, 2022.

BACKGROUND: It is unknown whether COVID-19 patients are at higher risk due to demographic and clinical characteristics associated with higher COVID-19 infection risk and severity of infection, or due to the disease and its management. AIM: To assess the impact of COVID-19 on healthcare-associated infection (HAI) transmission and antimicrobial use (AMU) prevalence during the later stages of the pandemic. METHODS: A point-prevalence survey (PPS) was conducted among 325 acute care hospitals of 19 out of 21 Regions of Italy, during November 2022. Non-COVID-19 patients were matched to COVID-19 patients according to age, sex, and severity of underlying conditions. HAI and AMU prevalence were calculated as the percentage of patients with at least one HAI or prescribed at least one antimicrobial over all included patients, respectively. FINDINGS: In total, 60,403 patients were included, 1897 (3.14%) of which were classified as COVID-19 patients. Crude HAI prevalence was significantly higher among COVID-19 patients compared to non-COVID-19 patients (9.54% vs 8.01%; prevalence rate ratio (PRR): 1.19; 95% confidence interval (CI): 1.04-1.38; P < 0.05), and remained higher in the matched sample; however, statistical significance was not maintained (odds ratio (OR): 1.25; 95% CI: 0.99-1.59; P = 0.067). AMU prevalence was significantly higher among COVID-19 patients prior to matching (46.39% vs 41.52%; PRR: 1.21; 95% CI: 1.11-1.32; P < 0.001), and significantly lower after matching (OR: 0.77; 95% CI: 0.66-0.89; P < 0.001). CONCLUSION: COVID-19 patients could be at higher HAI risk due to underlying clinical conditions and the intensity of healthcare needs. Further efforts should be dedicated to antimicrobial stewardship among COVID-19 patients.

Illustrating the processability of magnetic layered double hydroxides: layer-by-layer assembly of magnetic ultrathin films.

We report the preparation of single-layer layered double hydroxide (LDH) two-dimensional (2D) nanosheets by exfoliation of highly crystalline NiAl-NO3 LDH. Next, these unilamellar moieties have been incorporated layer-by-layer (LbL) into a poly(sodium 4-styrenesulfonate)/LDH nanosheet multilayer ultrathin film (UTF). Fourier transform infrared spectroscopy (FT-IR), ultraviolet-visible light (UV-vis), and X-ray diffraction (XRD) profiles have been used to follow the uniform growth of the UTF. The use of a magnetic LDH as the cationic component of the multilayered architecture enables study of the resulting magnetic properties of the UTFs. Our magnetic data show the appearance of spontaneous magnetization at ∼5 K, thus confirming the effective transfer of the magnetic properties of the bulk LDH to the self-assembled film that displays glassy-like ferromagnetic behavior. The high number of bilayers accessible-more than 80-opens the door for the preparation of more-complex hybrid multifunctional materials that combine magnetism with the physical properties provided by other exfoliable layered inorganic hosts.

Small-pore driven high capacitance in a hierarchical carbon via carbonization of Ni-MOF-74 at low temperatures.

A hierarchical porous carbon prepared via direct carbonization of Ni-MOF-74 loaded with furfuryl alcohol at 450 °C displays high specific capacitance in comparison with other MOF-derived carbons as a result of the formation of micropores smaller than 1 nm.

Side-chain control of porosity closure in single- and multiple-peptide-based porous materials by cooperative folding.

Porous materials are attractive for separation and catalysis-these applications rely on selective interactions between host materials and guests. In metal-organic frameworks (MOFs), these interactions can be controlled through a flexible structural response to the presence of guests. Here we report a MOF that consists of glycyl-serine dipeptides coordinated to metal centres, and has a structure that evolves from a solvated porous state to a desolvated non-porous state as a result of ordered cooperative, displacive and conformational changes of the peptide. This behaviour is driven by hydrogen bonding that involves the side-chain hydroxyl groups of the serine. A similar cooperative closure (reminiscent of the folding of proteins) is also displayed with multipeptide solid solutions. For these, the combination of different sequences of amino acids controls the framework's response to the presence of guests in a nonlinear way. This functional control can be compared to the effect of single-point mutations in proteins, in which exchange of single amino acids can radically alter structure and function.