COVID-19 and emergency department volume: The patients return but have different characteristics.

BACKGROUND: The COVID-19 pandemic has altered behaviors in the general population, as well as processes in the healthcare industry. Patients may be afraid to pursue care in the emergency department (ED) due to perceived risk of infection. The objective of this study was to determine the impact of COVID-19 on ED metrics. METHODS: At one metropolitan trauma center ED, we conducted a review of all visits from February to May in 2020 and compared findings with the same months from 2019. RESULTS: A total of 34,213 ED visits occurred during the study periods (18,471 in 2019 and 15,742 in 2020), with a decline in patient visits occurring after state emergency declarations. In 2020, patients were less likely to be female and more likely to arrive by ambulance. Diagnoses in the musculoskeletal, neurologic, and genitourinary categories occurred in lower proportions in 2020; toxicology, psychiatry, and infectious diseases occurred in higher proportions. In contrast to other insurance categories, Medicare patients comprised a larger share of ED visits in 2020 compared to 2019. DISCUSSION: Despite relatively low local prevalence of COVID-19, we report decreases in ED volume for some medical diagnosis categories. A volume rebound occurred in May 2020, but did not reach 2019 levels. Public health officials should encourage local populations to seek emergency care when concerned, and could consider programs to provide transportation. Patients should continue to protect themselves with social distancing and masks.

Solution structure of the nucleotide hydrolase BlsM: Implication of its substrate specificity.

Biosynthesis of the peptidyl nucleoside antifungal agent blasticidin S in Streptomyces griseochromogenes requires the hydrolytic function of a nucleotide hydrolase, BlsM, to excise the free cytosine from the 5'-monophosphate cytosine nucleotide. In addition to its hydrolytic activity, interestingly, BlsM has also been shown to possess a novel cytidine deaminase activity, converting cytidine, and deoxycytidine to uridine and deoxyuridine. To gain insight into the substrate specificity of BlsM and the mechanism by which it performs these dual function, the solution structure of BlsM was determined by multi-dimensional nuclear magnetic resonance approaches. BlsM displays a nucleoside deoxyribosyltransferase-like dimeric topology, with each monomer consisting of a five-stranded ß-sheet that is sandwiched by five α-helixes. Compared with the purine nucleotide hydrolase RCL, each monomer of BlsM has a smaller active site pocket, enclosed by a group of conserved hydrophobic residues from both monomers. The smaller size of active site is consistent with its substrate specificity for a pyrimidine, whereas a much more open active site, as in RCL might be required to accommodate a larger purine ring. In addition, BlsM confers its substrate specificity for a ribosyl-nucleotide through a key residue, Phe19. When mutated to a tyrosine, F19Y reverses its substrate preference. While significantly impaired in its hydrolytic capability, F19Y exhibited a pronounced deaminase activity on CMP, presumably due to an altered substrate orientation as a result of a steric clash between the 2'-hydroxyl of CMP and the ζ-OH group of F19Y. Finally, Glu105 appears to be critical for the dual function of BlsM.