RESUMO
BACKGROUND: The U.S. Centers for Disease Control and Prevention (CDC) defines legal intervention injuries as injuries caused by law enforcement agents in the course of official duties. Public health databases utilize International Classification of Diseases, 10th Revision (ICD-10), coding to collect these data through the "Y35" family ICD-10 code. Prior studies report deficiencies in public health recording of fatal legal intervention injuries. Few studies have characterized nonfatal injuries. This study investigates emergency department (ED) capture of legal intervention injury diagnostic coding. METHODS: A retrospective chart review was performed on ED encounter data from January 1, 2017, to June 30, 2019, at an academic hospital in Washington, DC. Charts were identified using a keyword search program for "police." Chart abstracters reviewed the flagged charts and abstracted those that met injury definition. Primary outcomes included injury severity, patient demographics, and documented ICD-10 codes. One sample proportion testing was performed comparing sample census ED data. RESULTS: A total of 340 encounters had sufficient descriptions of legal intervention injuries. A total of 259 had descriptions consistent with the patient specifier of "suspect." Hospital coders recorded 74 charts (28.6%) with the Y35 family legal intervention injury code. A total of 212 involved a Black patient. A total of 122 patients had Medicaid and 94 were uninsured. Black patients made up a higher proportion of individuals in the "suspect identified legal intervention injury" group than the total population (0.819 vs. 0.609, p < 0.01, 95% CI 0.772-0.866). Patients with Medicaid or who were uninsured made up substantial proportions as well (0.471 vs. 0.175, p < 0.01, 95% CI 0.410-0.532 for Medicaid patients and 0.363 vs. 0.155, p < 0.01, 95% CI 0.304-0.424 for the uninsured patients). CONCLUSION: A large proportion of nonfatal legal intervention injuries remain unreported. Black and low-income patients are disproportionately affected. More research is needed but benefits from interprofessional data sharing, injury pattern awareness, and diagnostic coding guidance may improve reporting.
RESUMO
Pterins are ubiquitous biomolecules with diverse functions including roles as cofactors, pigments, and redox mediators. Recently, a novel pterin-dependent signaling pathway that controls biofilm formation was identified in the plant pathogen, Agrobacterium tumefaciens A key player in this pathway is a pteridine reductase termed PruA, where its enzymatic activity has been shown to control surface attachment and limit biofilm formation. Here, we biochemically characterize PruA to investigate the catalytic properties and substrate specificity of this pteridine reductase. PruA demonstrates maximal catalytic efficiency with dihydrobiopterin and comparable activities with the stereoisomers dihydromonapterin and dihydroneopterin. Since A. tumefaciens does not synthesize or utilize biopterins, the likely physiological substrate is dihydromonapterin or dihydroneopterin, or both. Notably, PruA does not exhibit pteridine reductase activity with dihydrofolate or fully oxidized pterins. Site-directed mutagenesis studies of a conserved tyrosine residue, the key component of a putative catalytic triad, indicate that this tyrosine is not directly involved in PruA catalysis but may be important for substrate or cofactor binding. Additionally, mutagenesis of the arginine residue in the N-terminal TGX3RXG motif significantly reduces the catalytic efficiency of PruA, supporting its proposed role in pterin binding and catalysis. Finally, we report the enzymatic characterization of PruA homologs from Pseudomonas aeruginosa and Brucella abortus, thus expanding the roles and potential significance of pteridine reductases in diverse bacteria.Importance Biofilms are complex multicellular communities that are formed by diverse bacteria. In the plant pathogen, Agrobacterium tumefaciens, the transition from a free-living motile state to a non-motile biofilm state is governed by a novel signaling pathway involving small molecules called pterins. The involvement of pterins in biofilm formation is unexpected and prompts many questions about the molecular details of this pathway. This work biochemically characterizes the PruA pteridine reductase involved in the signaling pathway to reveal its enzymatic properties and substrate preference, thus providing important insight into pterin biosynthesis and its role in A. tumefaciens biofilm control. Additionally, the enzymatic characteristics of related pteridine reductases from mammalian pathogens are examined to uncover potential roles of these enzymes in other bacteria.
