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Implementing antimicrobial stewardship programs (ASPs) can be challenging due to prescriber resistance. Although barriers to implementing new ASPs have been identified, little is known about how prescribers perceive established programs. This information is critical to promoting the sustainability of ASPs.
To identify how prescribers perceive an established pediatric inpatient ASP that primarily utilizes prior authorization.
We conducted a cross-sectional survey administered from February through June 2017 in a large children’s hospital. The survey contained closed- and open-ended questions. Descriptive statistics and thematic content analysis approaches were used to analyze responses.
Of 394 prescribers invited, 160 (41%) responded. Prescribers had an overall favorable impression of the ASP, believing that it improves the quality of care (92.4% agree) and takes their judgment seriously (73.8%). The most common criticism of the ASP was that it threatened efficiency (26.0% agreed). In addition, 68.7% of respondents reported occasionally engaging in workarounds. Analysis of 133 free-text responses revealed that prescribers perceived that interacting with the ASP involved too many phone calls, caused communication breakdowns with the dispensing pharmacy, and led to gaps between approval and dispensing of antibiotics. Reasons given for workarounds included not wanting to change therapy that appears to be working, consultant disagreement with ASP recommendations, and the desire to do everything possible for patients.
Prescribers had a generally favorable opinion of an established ASP but found aspects to be inefficient. They reported engaging in workarounds occasionally for social and emotional reasons. Established ASPs should elicit feedback from frontline prescribers to optimize program impact.
This report describes the cloning and characterization of a pseudouridine (Ψ) synthase from mouse that we have named mouse pseudouridine synthase 1 (mpus1p). The cDNA is ∼1.5 kb and when used as a probe on a Northern blot of mouse RNA from tissues and cultured cells, several bands were detected. The open reading frame is 393 amino acids and has 35% identity over its length with yeast Ψ synthase 1 (pus1p). The recombinant protein was expressed in Escherichia coli and the purified protein converted specific uridines to Ψ in a number of tRNA substrates. The positions modified in stoichiometric amounts in vitro were 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA. A human cDNA was also cloned and the smaller open reading frame (348 amino acids) was 92% identical over its length with mpus1p but is shorter by 45 amino acids at the amino terminus. The expressed recombinant human protein has no activity on any of the tRNA substrates, most probably the result of the truncated open reading frame.
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