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Background: Nighttime sleep disruptions negatively impact the experience of hospitalized patients., Objective: To determine the impact of adopting a sleep-promoting nighttime clinical workflow for hospitalized patients on nocturnal disruptions and sleep., Design: Survey-based pre- and post-intervention cross-sectional study using convenience samples., Participants: Hospitalized veterans on a 23-bed general medical ward at a tertiary Veterans Administration Hospital., Interventions: Baseline sleep surveys (N=149) identified two major sources of interruptions: blood pressure checks at 4 am for telemetry patients and subcutaneous (SQ) heparin injections between 4:30 and 6 am for venous thromboembolism prophylaxis. Clinical workflow was restructured to eliminate these disruptions: moving 4 am blood pressure checks to 6 am and providing daily SQ enoxaparin at 9 am as an alternative to Q 8-h SQ heparin, which had prompted an injection between 4:30 and 6 am. The impact of these changes was assessed in a second round of surveys (N=99)., Main Measures: Frequency and sources for nighttime sleep disruptions; percentage of patients reporting longer time to fall asleep, more interruptions, and worse sleep quality (vs. home) before and after restructuring nighttime clinical workflow., Key Results: After restructuring nighttime clinical workflow, medication administration as a source of nighttime disruption decreased from 40% (59/149) to 4% (4/99) (p<0.001). Blood pressure checks as a source of disruption decreased from 56% (84/149) to 42% (42/99) (p=0.033). Fewer patients reported taking longer to fall asleep in the hospital vs. home (39% pre-intervention vs. 25% post-intervention, p=0.021). Similarly, fewer patients experienced waking up more frequently in the hospital vs. home (46% pre-intervention vs. 32% post-intervention, p=0.036). Fewer patients reported sleeping worse in the hospital (44% pre-intervention vs. 39% post-intervention), though this trend was not statistically significant (p=0.54)., Conclusions: Nighttime disruptions in hospitalized patients frequently interfere with sleep. Restructuring of the clinical workflow significantly reduced disruptions and improved sleep., (© 2023. This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply.)

Ferritin-like proteins form a novel family of bacterial proteins with diverse functions, such as DNA binding, iron storage and cell activation. A common structural feature of these proteins is their ability to form spherical dodecamers. Dpr is a ferritin-like protein from the Gram-positive bacterium Streptococcus suis. Full-length and truncated Dpr were expressed and purified as 6xHis-tag fusion proteins. Crystals of truncated Dpr suitable for X-ray diffraction analysis were obtained after the removal of the N-terminal affinity tag by thrombin cleavage. A complete data set to 2.3 A resolution was collected using synchrotron radiation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 104.3, b = 137.6, c = 142.1 A and 12 molecules in the asymmetric unit.

Streptococcus suis causes meningitis and other serious infections in pigs and humans, and binds to host cell globotriosylceramide. In order to determine the essential hydroxyls involved in binding, the complete set of monodeoxy derivatives of the receptor trisaccharide Gal alpha1-Gal beta1-4Glc were tested as inhibitors of bacterial hemagglutination. Removal of the 4''-, 6'', 2' or 3'-hydroxyls abolished inhibitory activity, which indicated that they were critically involved in binding. The same results were obtained using synthetic lipid-linked monodeoxy derivatives of the trisaccharides in a thin-layer overlay assay. The P(N) and P(O) subtypes of the S. suis adhesin showed similar binding patterns. The hydroxyls of the glucose moiety were not critical for binding, although the adhesin binds better to the trisaccharide Gal alpha1-4Gal beta1-4Glc than the disaccharide Gal alpha1-4Gal.

Streptococcus suis causes septicaemia and meningitis in pigs and occasionally in humans. A major galactose-inhibitable adhesin recognizing the blood group P-related disaccharide Gal alpha 1-4 Gal beta 1--present in the GbO3 glycolipid was identified in S. suis. Two variant adhesins, inhibitable by galactose and N-acetylgalactosamine (type PN) or galactose only (type Po) both preferred the disaccharide in terminal position. The hydrogen bonding patterns were determined using deoxy and other derivatives of the receptor disaccharide, and were compared to that of E. coli PapG396 adhesin. The essential hydroxyls were the HO-4', HO-6', HO-2 and HO-3 hydroxyls; type Po adhesin also weakly interacted with HO-6 and HO-3'. The mechanism differed from that of E. coli which binds to a cluster of five hydroxyls, HO-6, HO-2', HO-3', HO-4' and HO-6'. The purified adhesin had a molecular weight of 18 kDa and an isoelectric point of 6.4. The agglutination of latex-bound purified adhesin was inhibited by the same inhibitors as agglutination with whole bacteria. The adhesin was detected by immunoblot analysis in all 23 S. suis strains examined representing different serotypes, was highly immunogenic and showed opsonizing activity. This represents the first example of the comparison of the saccharide receptor hydrogen bondings of two bacteria of different origin and shows that the same saccharide may be recognised by two different mechanisms. As a potential virulence factor present in different serotypes the adhesin represents a potential vaccine against S. suis infections.