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Background: Reducing bronchopulmonary dysplasia (BPD) utilizing a single intervention has been challenging. The quality improvement (QI) bundle approach may better address BPD multifactorial risk factors., Methods: A single-center interdisciplinary quality improvement (QI) initiative to enhance respiratory care for preterm infants born less than 30 weeks gestation., Global Aim: To reduce BPD in preterm infants., Smart Aim: Introduce and implement a comprehensive, evidence-based respiratory care bundle within 12 months, targeting areas needing improvement in our practices., Results: Our preplanned improvement targets were achieved for all process measures. Overall BPD incidence did not change (45% vs. 44.3%). After the QI intervention, inborn infants had a lower BPD rate, though not statistically significant (38.7% vs. 30.3%, p = 0.22), with a significant reduction in grade 1 BPD (24.5% vs. 12.4%, p = 0.032)., Conclusion: Structured interdisciplinary QI work tailored to local settings can improve respiratory care and possibly amend the outcomes of infants at risk for BPD., Competing Interests: Competing interests: The authors declare no competing interests. Ethics: CHOC’s institutional review board reviewed the project and determined that it did not meet the requirements for human subject research., (© 2024. The Author(s), under exclusive licence to Springer Nature America, Inc.)

Translational G proteins, whose release from the ribosome is triggered by GTP hydrolysis, regulate protein synthesis. Concomitantly with binding and dissociation of protein factors, translation is accompanied by forward and reverse rotation between ribosomal subunits. Using single-molecule measurements, we explore the ways in which the binding of translational GTPases affects inter-subunit rotation of the ribosome. We demonstrate that the highly conserved translation factor LepA, whose function remains debated, shifts the equilibrium toward the non-rotated conformation of the ribosome. By contrast, the catalyst of ribosome translocation, elongation factor G (EF-G), favors the rotated conformation of the ribosome. Nevertheless, the presence of P-site peptidyl-tRNA and antibiotics, which stabilize the non-rotated conformation of the ribosome, only moderately reduces EF-G binding. These results support the model suggesting that EF-G interacts with both the non-rotated and rotated conformations of the ribosome during mRNA translocation. Our results provide new insights into the molecular mechanisms of LepA and EF-G action and underscore the role of ribosome structural dynamics in translation.

Background: Streptococcus agalactiae (group B Streptococcus [GBS]) asymptomatically colonizes approximately 20% of adults; however, GBS causes severe disease in susceptible populations, including newborns, pregnant women, and elderly individuals. In shifting between commensal and pathogenic states, GBS reveals multiple mechanisms of virulence factor control. Here we describe a GBS protein that we named "biofilm regulatory protein A" (BrpA) on the basis of its homology with BrpA from Streptococcus mutans., Methods: We coupled phenotypic assays, RNA sequencing, human neutrophil and whole-blood killing assays, and murine infection models to investigate the contribution of BrpA to GBS physiology and virulence., Results: Sequence analysis identified BrpA as a LytR-CpsA-Psr enzyme. Targeted mutagenesis yielded a GBS mutant (ΔbrpA) with normal ultrastructural morphology but a 6-fold increase in chain length, a biofilm defect, and decreased acid tolerance. GBS ΔbrpA stimulated increased neutrophil reactive oxygen species and proved more susceptible to human and murine blood and neutrophil killing. Notably, the wild-type parent outcompeted ΔbrpA GBS in murine sepsis and vaginal colonization models. RNA sequencing of ΔbrpA uncovered multiple differences from the wild-type parent, including pathways of cell wall synthesis and cellular metabolism., Conclusions: We propose that BrpA is an important virulence regulator and potential target for design of novel antibacterial therapeutics against GBS.