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Background/objective: The coronavirus disease 2019 (COVID-19) pandemic has challenged the ability of Emergency Medical Services (EMS) providers to maintain personal safety during the treatment and transport of patients potentially infected. Increased rates of COVID-19 infection in EMS providers after patient care exposure, and notably after performing aerosol-generating procedures (AGPs), have been reported. With an already strained workforce seeing rising call volumes and increased risk for AGP-requiring patient presentations, development of novel devices for the protection of EMS providers is of great importance.Based on the concept of a negative pressure room, the AerosolVE BioDome is designed to encapsulate the patient and contain aerosolized infectious particles produced during AGPs, making the cabin of an EMS vehicle safer for providers. The objective of this study was to determine the efficacy and safety of the tent in mitigating simulated infectious particle spread in varied EMS transport platforms during AGP utilization., Methods: Fifteen healthy volunteers were enrolled and distributed amongst three EMS vehicles: a ground ambulance, an aeromedical-configured helicopter, and an aeromedical-configured jet. Sodium chloride particles were used to simulate infectious particles and particle counts were obtained in numerous locations close to the tent and around the patient compartment. Counts near the tent were compared to ambient air with and without use of AGPs (non-rebreather mask, continuous positive airway pressure [CPAP] mask, and high-flow nasal cannula [HFNC])., Results: For all transport platforms, with the tent fan off, the particle generator alone, and with all AGPs produced particle counts inside the tent significantly higher than ambient particle counts (P <.0001). With the tent fan powered on, particle counts near the tent, where EMS providers are expected to be located, showed no significant elevation compared to baseline ambient particle counts during the use of the particle generator alone or with use of any of the AGPs across all transport platforms., Conclusion: Development of devices to improve safety for EMS providers to allow for use of all available therapies to treat patients while reducing risk of communicable respiratory disease transmission is of paramount importance. The AerosolVE BioDome demonstrated efficacy in creating a negative pressure environment and workspace around the patient and provided significant filtration of simulated respiratory droplets, thus making the confined space of transport vehicles potentially safer for EMS personnel.

Background/objective: The coronavirus disease 2019 (COVID-19) pandemic has created challenges in maintaining the safety of prehospital providers caring for patients. Reports have shown increased rates of Emergency Medical Services (EMS) provider infection with COVID-19 after patient care exposure, especially while utilizing aerosol-generating procedures (AGPs). Given the increased risk and rising call volumes for AGP-necessitating complaints, development of novel devices for the protection of EMS clinicians is of great importance.Drawn from the concept of the powered air purifying respirator (PAPR), the AerosolVE helmet creates a personal negative pressure space to contain aerosolized infectious particles produced by patients, making the cabin of an EMS vehicle safer for providers. The helmet was developed initially for use in hospitals and could be of significant use in the prehospital setting. The objective of this study was to determine the efficacy and safety of the helmet in mitigating simulated infectious particle spread in varied EMS transport platforms during AGP utilization., Methods: Fifteen healthy volunteers were enrolled and distributed amongst three EMS vehicles: a ground ambulance, a medical helicopter, and a medical jet. Sodium chloride particles were used to simulate infectious particles, and particle counts were obtained in numerous locations close to the helmet and around the patient compartment. Counts near the helmet were compared to ambient air with and without use of AGPs (non-rebreather mask [NRB], continuous positive airway pressure mask [CPAP], and high-flow nasal cannula [HFNC])., Results: Without the helmet fan on, the particle generator alone and with all AGPs produced particle counts inside the helmet significantly higher than ambient particle counts. With the fan on, there was no significant difference in particle counts around the helmet compared to baseline ambient particle counts. Particle counts at the filter exit averaged less than one despite markedly higher particle counts inside the helmet., Conclusion: Given the risk to EMS providers by communicable respiratory diseases, development of devices to improve safety while still enabling use of respiratory therapies is of paramount importance. The AerosolVE helmet demonstrated efficacy in creating a negative pressure environment and provided significant filtration of simulated respiratory droplets, thus making the confined space of transport vehicles potentially safer for EMS personnel.

The dynamic properties of ribosomal protein L9 from Bacillus stearothermophilus were investigated in solution using an analysis of nitrogen-15 longitudinal and transverse relaxation rates and amide nitrogen-proton nuclear Overhauser effects. The relaxation rates of the amide nitrogen nuclei were found to be correlated with the angle between the amide nitrogen-proton bond vectors and the long axis of the protein. This directional dependence of the nuclear relaxation rates is consistent with the protein having a highly elongated shape in solution, consistent with that observed in previous X-ray crystallographic studies of the crystalline form. Analysis of the nuclear relaxation data shows that the solvent-exposed nine-turn alpha helix connecting the two domains has a relatively high degree of order, in contrast to the connecting helix in the similarly shaped, but functionally different, calmodulin protein. The rotational correlation times associated with the amide nitrogen atoms of the N-terminal domain are on average slightly shorter than those of the C-terminal domain and connecting helix, providing evidence that the N-terminal domain exhibits some degree of independence in tumbling, in addition to other fast internal motions. The putative RNA-binding surfaces in each of the protein domains are characterized by relatively low order parameters, indicating that these are the most flexible regions of the molecule. Overall, the picture of the internal dynamics provided by nuclear relaxation measurements is similar to that obtained from a detailed study of amide proton exchange rates, but differs markedly from the picture provided by crystallographic temperature factors. The present study describes a molecule with unusual and complex dynamic properties, and supports a model where the protein functions as a "molecular strut" within the ribosome., (Copyright 1998 Academic Press.)

Nuclear magnetic resonance and circular dichroism experiments were used to investigate the stability and dynamic aspects of ribosomal protein L9 from Bacillus stearothermophilus in solution. This unusually shaped protein, with its two widely spaced RNA-binding domains linked by a connecting helix, has been hypothesized to serve as a "molecular strut", most likely playing a role in ribosome assembly and/or maintaining the catalytically active conformation of ribosomal RNA. Protection factors for amide proton exchange were quantitatively measured in an extensive series of NMR experiments, providing probes of the stability and dynamics of localized regions of the protein. Results show that each of the two RNA-binding domains contains a highly stable core. The exposed central helix that connects the two domains is helical in solution, albeit not rigid, a result that is supported by amide proton protection factors, circular dichroism measurements, and carbon-13 and proton chemical shift index values. A conserved glycine and lysine-rich loop in the N-terminal domain is ordered and quite stable, a surprising result, since this loop had been presumed to be disordered in the original crystallographic analysis. Interestingly, the most dynamic parts of the protein are the regions that contain the likely RNA-binding residues in each of the two domains. The present results add further support to the notion that the L9 protein plays an architectural role within the ribosome, with the central helix serving as a molecular strut, or perhaps a spring, linking the two widely spaced RNA-binding domains.