A Quality Improvement Initiative to Decrease Central Line-Associated Bloodstream Infections During the COVID-19 Pandemic: A "Zero Harm" Approach.

INTRODUCTION: Central line-associated bloodstream infections (CLABSIs) are associated with significant patient harm and health care costs. Central line-associated bloodstream infections are preventable through quality improvement initiatives. The COVID-19 pandemic has caused many challenges to these initiatives. Our community health system in Ontario, Canada, had a baseline rate of 4.62 per 1000 line days during the baseline period. OBJECTIVES: Our aim was to reduce CLABSIs by 25% by 2023. METHODS: An interprofessional quality aim committee performed a root cause analysis to identify areas for improvement. Change ideas included improving governance and accountability, education and training, standardizing insertion and maintenance processes, updating equipment, improving data and reporting, and creating a culture of safety. Interventions occurred over 4 Plan-Do-Study-Act cycles. The outcome was CLABSI rate per 1000 central lines: process measures were rate of central line insertion checklists used and central line capped lumens used, and balancing measure was the number of CLABSI readmissions to the critical care unit within 30 days. RESULTS: Central line-associated bloodstream infections decreased over 4 Plan-Do-Study-Act cycles from a baseline rate of 4.62 (July 2019-February 2020) to 2.34 (December 2021-May 2022) per 1000 line days (51%). The rate of central line insertion checklists used increased from 22.8% to 56.9%, and central line capped lumens used increased from 72% to 94.3%. Mean CLABSI readmissions within 30 days decreased from 1.49 to 0.1798. CONCLUSIONS: Our multidisciplinary quality improvement interventions reduced CLABSIs by 51% across a health system during the COVID-19 pandemic.

Making change easy: A peer-to-peer guide on transitioning to new hand hygiene products.

This report summarizes our experiences planning and implementing the transition to a new commercial line of hand hygiene products and their dispensing systems in a large academic health care facility in Toronto, Canada. Our lessons learned are organized into a practical guide made available in 2 different formats: this article and an illustrated peer-to-peer guide (http://www.baycrest.org/wp-content/uploads/HCE-PROG-HH_HighQuality.pdf).

Impact of chlorhexidine bathing on methicillin-resistant Staphylococcus aureus incidence in an endemic chronic care setting: A randomized controlled trial.

We postulated that bathing with 2% chlorhexidine-impregnated antiseptic washcloths could reduce methicillin-resistant Staphylococcus aureus (MRSA) incidence among chronic care patients compared with nonantiseptic bathing. A total of 122 patients on 3 hospital units were enrolled in a 12-month, cluster-randomized, open-label, controlled trial, with 8 patients becoming MRSA positive. The 2% chlorhexidine-impregnated antiseptic washcloths reduced incidence by 71% (0.1 vs 0.44 cases per 1,000 patient days) (P = .14; Fisher exact). The detected difference was not statistically significant because of a low number of observed events.

Identification of different clonal complexes and diverse amino acid substitutions in penicillin-binding protein 2 (PBP2) associated with borderline oxacillin resistance in Canadian Staphylococcus aureus isolates.

Borderline oxacillin-resistant Staphylococcus aureus (BORSA) exhibit oxacillin MIC values of 1-8 microg ml(-1), but lack mecA, which encodes the low-affinity penicillin-binding protein (PBP)2a. The relationship of the BORSA phenotype with specific genetic backgrounds was assessed, as well as amino acid sequence variation in the normal PBP2. Among 38 BORSA, 26 had a common PFGE profile of genomic DNA, and were multilocus sequence type (ST)25. The other isolates were genetically diverse. Complete pbp2 sequences were determined for three BORSA, corresponding to ST25, ST1 and ST47, which were selected on the basis of lacking blaZ-encoded beta-lactamase. The essential transpeptidase-domain-encoding segment of pbp2 was also sequenced from seven additional ST25 isolates. Amino acid substitutions occurred in the transpeptidase domain of all BORSA, irrespective of clonal type. A Gln(629)-->Pro substitution was common to all ST25 BORSA, but most could be distinguished from one another by additional unique substitutions in the transpeptidase domain. The ST1 and ST47 isolates also possessed unique substitutions in the transpeptidase domain. Plasmid-mediated expression of pbp2 from an ST25 or ST1 isolate in S. aureus RN6390 increased its oxacillin MIC from 0.25 to 4 microg ml(-1), while pbp2 from a susceptible strain, ATCC 25923, had no effect. Therefore, different amino acid substitutions in PBP2 of diverse BORSA lineages contribute to borderline resistance. The predominant ST25 lineage was not related to any of the five clonal complexes that contain meticillin-resistant S. aureus (MRSA), suggesting that ST25 cannot readily acquire mecA-mediated resistance.

A combination of micronutrients is beneficial in reducing the incidence of prostate cancer and increasing survival in the Lady transgenic model.

We have previously shown that administration of a combination of micronutrients (selenium, vitamin E, and lycopene) inhibits prostate cancer (PCa) development in the Lady transgenic model. In the present study, we examine timing of initiation of micronutrients, and the effect of micronutrient combinations, on PCa development in Lady transgenic model. Transgenic males were randomized to either a control diet; control diet supplemented with human equivalent doses of vitamin E, selenium, and lycopene (E+S+L); or control diet supplemented with vitamin E and selenium (E+S). In separate experiments, the combination of E+S+L was initiated at varying time points (4, 8, 20, and 36 weeks of age). A combination of E+S+L resulted in a significant reduction in PCa and liver metastasis when intervention was commenced within 8 weeks of age (P < 0.0001). Immunohistochemical analysis revealed a strong correlation between disease-free state with up-regulation of the prognostic marker p27(Kip1) (P < 0.0001) and decreased expression of proliferating cell nuclear antigen and significantly increased apoptotic index (P < 0.0001). On the contrary, a combination of E+S was not effectual in preventing PCa, with a high proportion (84.6%) of animals developing PCa and a small proportion (11.5%) developing high-grade PIN. Early commencement of micronutrients (E+S+L) is beneficial in reducing PCa. Lycopene is an essential component of the combination and effective (when used with E+S) for PCa prevention. These observations provide support for their chemopreventive effect and some clues about their mechanism of action. These key findings will be complementary to the outcome from the Selenium and Vitamin E Chemoprevention Trial.

Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing.

The serine and cysteine proteases SspA and SspB of Staphylococcus aureus are secreted as inactive zymogens, zSspA and zSspB. Mature SspA is a trypsin-like glutamyl endopeptidase and is required to activate zSspB. Although a metalloprotease Aureolysin (Aur) is in turn thought to contribute to activation of zSspA, a specific role has not been demonstrated. We found that pre-zSspA is processed by signal peptidase at ANA(29) downward arrow, releasing a Leu(30) isoform that is first processed exclusively through autocatalytic intramolecular cleavage within a glutamine-rich propeptide segment, (40)QQTQSSKQQTPKIQ(53). The preferred site is Gln(43) with secondary processing at Gln(47) and Gln(53). This initial processing is necessary for optimal and subsequent Aur-dependent processing at Leu(58) and then Val(69) to release mature SspA. Although processing by Aur is rate-limiting in zSspA activation, the first active molecules of Val(69)SspA promote rapid intermolecular processing of remaining zSspA at Glu(65), producing an N-terminal (66)HANVILP isoform that is inactive until removal of the HAN tripeptide by Aur. Modeling indicated that His(66) of this penultimate isoform blocks the active site by hydrogen bonding to Ser(237) and occlusion of substrate. Binding of glutamate within the active site of zSspA is energetically unfavorable, but glutamine fits into the primary specificity pocket and is predicted to hydrogen bond to Thr(232) proximal to Ser(237), permitting autocatalytic cleavage of the glutamine-rich propeptide segment. These and other observations suggest that zSspA is activated through a trypsinogen-like mechanism where supplementary features of the propeptide must be sequentially processed in the correct order to allow efficient activation.