Causes of early postpartum complications that result in visits to the emergency department.

OBJECTIVE: This study aimed to review the reasons why postpartum women present to the emergency department (ED) over a short term (≤10 days post-delivery) and to identify the risk factors associated with early visits to the ED. METHODS: This retrospective chart review included all women who delivered at a regional health system (William Osler Health System, WOHS) in 2018 and presented to the WOHS ED within 10 days after delivery. Baseline descriptive statistics were used to examine the patient demographics and identify the timing of the postpartum visit. Univariate tests were used to identify significant predictors for admission. A multivariate model was developed based on backward selection from these significant factors to identify admission predictors. RESULTS: There were 381 visits identified, and the average age of the patients was 31.22 years (SD: 4.83), with median gravidity of 2 (IQR: 1-3). Most patients delivered via spontaneous vaginal delivery (53.0%). The median time of presentation to the ED was 5.0 days, with the following most common reasons: abdominal pain (21.5%), wound-related issues (12.6%), and urinary issues (9.7%). Delivery during the weekend (OR 1.91, 95% CI 1.00-3.65, P = 0.05) was predictive of admission while Group B Streptococcus positive patients were less likely to be admitted (OR 0.22, CI 0.05-0.97, P<0.05). CONCLUSIONS: This was the first study in a busy community setting that examined ED visits over a short postpartum period. Patient education on pain management and wound care can reduce the rate of early postpartum ED visits.

Correction: Structure and functional analysis of a bacterial adhesin sugar-binding domain.

[This corrects the article DOI: 10.1371/journal.pone.0220045.].

Structure and functional analysis of a bacterial adhesin sugar-binding domain.

Bacterial adhesins attach their hosts to surfaces through one or more ligand-binding domains. In RTX adhesins, which are localized to the outer membrane of many Gram-negative bacteria via the type I secretion system, we see several examples of a putative sugar-binding domain. Here we have recombinantly expressed one such ~20-kDa domain from the ~340-kDa adhesin found in Marinobacter hydrocarbonoclasticus, an oil-degrading bacterium. The sugar-binding domain was purified from E. coli with a yield of 100 mg/L of culture. Circular dichroism analysis showed that the protein was rich in beta-structure, was moderately heat resistant, and required Ca2+ for proper folding. A crystal structure was obtained in Ca2+ at 1.2-Å resolution, which showed the presence of three Ca2+ ions, two of which were needed for structural integrity and one for binding sugars. Glucose was soaked into the crystal, where it bound to the sugar's two vicinal hydroxyl groups attached to the first and second (C1 and C2) carbons in the pyranose ring. This attraction to glucose caused the protein to bind certain polysaccharide-based column matrices and was used in a simple competitive binding assay to assess the relative affinity of sugars for the protein's ligand-binding site. Fucose, glucose and N-acetylglucosamine bound most tightly, and N-acetylgalactosamine hardly bound at all. Isothermal titration calorimetry was used to determine specific binding affinities, which lie in the 100-µM range. Glycan arrays were tested to expand the range of ligand sugars assayed, and showed that MhPA14 bound preferentially to branched polymers containing terminal sugars highlighted as strong binders in the competitive binding assay. Some of these binders have vicinal hydroxyl groups attached to the C3 and C4 carbons that are sterically equivalent to those presented by the C1 and C2 carbons of glucose.