Health Care Personnel Exposure Risk Assessment and Management During a Mpox Outbreak in Chicago, Illinois, 17 May to 8 July 2022.

This report summarizes risk assessment interviews and follow-up with health care personnel (HCP) after exposure to patients with mpox disease during 17 May to 8 July 2022. HCP-case interactions were assessed using a standard questionnaire to categorize the risk associated with patient encounters. We assessed 150 interactions among 142 HCP and 30 cases. Four (2.7%) interactions were defined as high risk, 5 (3.3%) intermediate, 107 (71.3%) low, and 31 (20.7%) no risk. High and intermediate exposures were offered postexposure prophylaxis; 4 accepted. No documented mpox transmission after exposure was identified. These findings suggest transmission risk in health care settings during routine patient care is low.

Structure-Based Analysis of Boronic Acids as Inhibitors of Acinetobacter-Derived Cephalosporinase-7, a Unique Class C ß-Lactamase.

Acinetobacter baumannii is a multidrug resistant pathogen that infects more than 12 000 patients each year in the US. Much of the resistance to ß-lactam antibiotics in Acinetobacter spp. is mediated by class C ß-lactamases known as Acinetobacter-derived cephalosporinases (ADCs). ADCs are unaffected by clinically used ß-lactam-based ß-lactamase inhibitors. In this study, five boronic acid transition state analog inhibitors (BATSIs) were evaluated for inhibition of the class C cephalosporinase ADC-7. Our goal was to explore the properties of BATSIs designed to probe the R1 binding site. Ki values ranged from low micromolar to subnanomolar, and circular dichroism (CD) demonstrated that each inhibitor stabilizes the ß-lactamase-inhibitor complexes. Additionally, X-ray crystal structures of ADC-7 in complex with five inhibitors were determined (resolutions from 1.80 to 2.09 Å). In the ADC-7/CR192 complex, the BATSI with the lowest Ki (0.45 nM) and greatest Δ Tm (+9 °C), a trifluoromethyl substituent, interacts with Arg340. Arg340 is unique to ADCs and may play an important role in the inhibition of ADC-7. The ADC-7/BATSI complexes determined in this study shed light into the unique recognition sites in ADC enzymes and also offer insight into further structure-based optimization of these inhibitors.