Acceptability and Preferences of Simulation-Based Continuing Education Among Emergency Medical Service Providers.

INTRODUCTION: Simulation-based education (SBE) has been shown to be an effective and accepted teaching modality across multiple fields of medical education. Prehospital systems currently utilize simulation for initial training; however, few studies have determined the acceptability for simulation-based training for continued education among emergency medical service (EMS) providers. METHODS: We performed a retrospective mixed method review of data from prehospital provider evaluations of high-fidelity SBE training sessions. Survey responses included questions on a Likert scale pertaining to acceptability of the training, as well as free-text comments. Providers included a mix of crews with varying levels of training. RESULTS: We received a 96% response rate for providers who completed the training. Participants rated simulation as an educational tool and the overall value of the session highly for EMS providers across all levels of training with no difference among training level. All providers also indicated they would like similar training on a frequent basis in the future. CONCLUSION: Simulation-based education was found to be an acceptable tool for EMS training and should be considered for use during continuing education for all levels of practicing EMS providers. In addition, EMS providers indicated a preference for participating in SBE on a frequent basis. EMS training programs should consider incorporating more frequent SBE.

Case Report of a Left-sided Superior Vena Cava Causing Unique Positioning of Central Line.

INTRODUCTION: Persistent left-sided superior vena cava is a rare congenital venous malformation. While often clinically asymptomatic, these variations in normal anatomy may give rise to complications with central venous catheter placement. CASE REPORT: We present a case of a 71-year-old male who presented to the emergency department with sepsis of unknown etiology. A right-sided central venous catheter was placed, and due to a persistent left-sided superior vena cava the post-procedure chest radiograph showed a uniquely positioned catheter tip within the left atrium. CONCLUSION: A persistent left-sided superior vena cava may lead to uniquely positioned catheter tip placement on post-procedural imaging. This case demonstrates the need to consider variants in normal venous anatomy, such as persistent left-sided superior vena cava, to aid with correct interpretation of post-procedure imaging findings.

Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N(5) -formyltetrahydrofolate and UDP-Ara4N.

ArnA from Escherichia coli is a key enzyme involved in the formation of 4-amino-4-deoxy-l-arabinose. The addition of this sugar to the lipid A moiety of the lipopolysaccharide of pathogenic Gram-negative bacteria allows these organisms to evade the cationic antimicrobial peptides of the host immune system. Indeed, it is thought that such modifications may be responsible for the repeated infections of cystic fibrosis patients with Pseudomonas aeruginosa. ArnA is a bifunctional enzyme with the N- and C-terminal domains catalyzing formylation and oxidative decarboxylation reactions, respectively. The catalytically competent cofactor for the formylation reaction is N(10) -formyltetrahydrofolate. Here we describe the structure of the isolated N-terminal domain of ArnA in complex with its UDP-sugar substrate and N(5) -formyltetrahydrofolate. The model presented herein may prove valuable in the development of new antimicrobial therapeutics.

Molecular structure of an N-formyltransferase from Providencia alcalifaciens O30.

The existence of N-formylated sugars in the O-antigens of Gram-negative bacteria has been known since the middle 1980s, but only recently have the biosynthetic pathways for their production been reported. In these pathways, glucose-1-phosphate is first activated by attachment to a dTMP moiety. This step is followed by a dehydration reaction and an amination. The last step in these pathways is catalyzed by N-formyltransferases that utilize N(10) -formyltetrahydrofolate as the carbon source. Here we describe the three-dimensional structure of one of these N-formyltransferases, namely VioF from Providencia alcalifaciens O30. Specifically, this enzyme catalyzes the conversion of dTDP-4-amino-4,6-dideoxyglucose (dTDP-Qui4N) to dTDP-4,6-dideoxy-4-formamido-d-glucose (dTDP-Qui4NFo). For this analysis, the structure of VioF was solved to 1.9 Å resolution in both its apoform and in complex with tetrahydrofolate and dTDP-Qui4N. The crystals used in the investigation belonged to the space group R32 and demonstrated reticular merohedral twinning. The overall catalytic core of the VioF subunit is characterized by a six stranded mixed ß-sheet flanked on one side by three α-helices and on the other side by mostly random coil. This N-terminal domain is followed by an α-helix and a ß-hairpin that form the subunit:subunit interface. The active site of the enzyme is shallow and solvent-exposed. Notably, the pyranosyl moiety of dTDP-Qui4N is positioned into the active site by only one hydrogen bond provided by Lys 77. Comparison of the VioF model to that of a previously determined N-formyltransferase suggests that substrate specificity is determined by interactions between the protein and the pyrophosphoryl group of the dTDP-sugar substrate.