Systematic Improvement in the Patient Transfer Process to a Tertiary Care Children's Hospital.

OBJECTIVE: Interfacility transfer of pediatric patients to a children's hospital is a complex process that can be time consuming and dissatisfying for referring providers. We aimed to improve the efficiency of communication and acceptance for interfacility transfers to our hospital. METHODS: We implemented iterative improvements to the process in 2 phases from 2013 to 2016 (pediatric medicine) and 2019 to 2022 (pediatric critical care and surgery). Key interventions included creation of a hospitalist position to manage transfers with broad ability to accept patients and transition to direct phone access for transfer requests to streamline connection. Effective initiatives from Phase 1 were adapted and spread to the other services in Phase 2. Data were manually extracted monthly from call transcripts and monitored by using statistical process control (SPC) charts. Primary outcome measures were time from call to connection to a provider and number of providers added to the call before making a disposition decision. RESULTS: Average time from call initiation to provider connection for pediatric medicine calls decreased from 11 minutes to 5 minutes. The average number of internal physicians on each call before acceptance decreased from 2.1 to 1.3. In Phase 2, time to provider connection decreased from 11 to 4 minutes for pediatric critical care calls and 16 to 5 minutes for pediatric surgery calls. CONCLUSIONS: We streamlined the process of accepting incoming transfer requests throughout our children's hospital. Prioritizing direct communication led to efficient disposition decisions and progression toward transfer and was effective for multiple service lines.

A Genetically Engineered Rotavirus NSP2 Phosphorylation Mutant Impaired in Viroplasm Formation and Replication Shows an Early Interaction between vNSP2 and Cellular Lipid Droplets.

Many RNA viruses replicate in cytoplasmic compartments (virus factories or viroplasms) composed of viral and cellular proteins, but the mechanisms required for their formation remain largely unknown. Rotavirus (RV) replication in viroplasms requires interactions between virus nonstructural proteins NSP2 and NSP5, which are associated with components of lipid droplets (LDs). We previously identified two forms of NSP2 in RV-infected cells, a cytoplasmically dispersed form (dNSP2) and a viroplasm-specific form (vNSP2), which interact with hypophosphorylated and hyperphosphorylated NSP5, respectively, indicating that a coordinated phosphorylation cascade controls viroplasm assembly. The cellular kinase CK1α phosphorylates NSP2 on serine 313, triggering the localization of vNSP2 to sites of viroplasm assembly and its association with hyperphosphorylated NSP5. Using reverse genetics, we generated a rotavirus with a phosphomimetic NSP2 (S313D) mutation to directly evaluate the role of CK1α NSP2 phosphorylation in viroplasm formation. Recombinant rotavirus NSP2 S313D (rRV NSP2 S313D) is significantly delayed in viroplasm formation and in virus replication and interferes with wild-type RV replication in coinfection. Taking advantage of the delay in viroplasm formation, the NSP2 phosphomimetic mutant was used as a tool to observe very early events in viroplasm assembly. We show that (i) viroplasm assembly correlates with NSP5 hyperphosphorylation and (ii) vNSP2 S313D colocalizes with RV-induced LDs without NSP5, suggesting that vNSP2 phospho-S313 is sufficient for interacting with LDs and may be the virus factor required for RV-induced LD formation. Further studies with the rRV NSP2 S313D virus are expected to reveal new aspects of viroplasm and LD initiation and assembly.IMPORTANCE Reverse genetics was used to generate a recombinant rotavirus with a single phosphomimetic mutation in nonstructural protein 2 (NSP2 S313D) that exhibits delayed viroplasm formation, delayed replication, and an interfering phenotype during coinfection with wild-type rotavirus, indicating the importance of this amino acid during virus replication. Exploiting the delay in viroplasm assembly, we found that viroplasm-associated NSP2 colocalizes with rotavirus-induced lipid droplets prior to the accumulation of other rotavirus proteins that are required for viroplasm formation and that NSP5 hyperphosphorylation is required for viroplasm assembly. These data suggest that NSP2 phospho-S313 is sufficient for interaction with lipid droplets and may be the virus factor that induces lipid droplet biogenesis in rotavirus-infected cells. Lipid droplets are cellular organelles critical for the replication of many viral and bacterial pathogens, and thus, understanding the mechanism of NSP2-mediated viroplasm/lipid droplet initiation and interaction will lead to new insights into this important host-pathogen interaction.

Genome Sequences of 19 Novel Erwinia amylovora Bacteriophages.

Erwinia amylovora is the causal agent of fire blight, a devastating disease affecting some plants of the Rosaceae family. We isolated bacteriophages from samples collected from infected apple and pear trees along the Wasatch Front in Utah. We announce 19 high-quality complete genome sequences of E. amylovora bacteriophages.