Diabetes Education with a Teaching Kitchen Intervention Can Improve Hemoglobin A1c for Type 2 Diabetics Compared to Traditional Diabetes Education

AuthorsJill Christensen MD MPH Providence Milwaukie HospitalHeidi Davis MSW Providence Milwaukie HospitalCharlotte Navarre RN Providence Milwaukie HospitalHsin-Fang Li PHD Providence Medical Data Research CenterKathy Schwab MPH RDN Providence Health EducationRichard O’Neil MBA Providence Planning Analyst Title Diabetes Education with a Teaching Kitchen Intervention Can Improve Hemoglobin A1c for Type 2 Diabetics Compared to Traditional Diabetes Education Purpose The Providence Milwaukie Community Teaching Kitchen offers health-focused, budget friendly cooking classes for patients. In 2019, we piloted diabetes education classes with an added hands-on culinary session. This study compares the change in hemoglobin A1c for patients who participated in the pilot with those in the standard curriculum and those referred to diabetes education but did not enroll. Methods This retrospective analysis compared change in hemoglobin A1c for all patients referred to diabetes education in the Providence Northern Oregon region in 2019. Patients referred to diabetes education but not enrolled were considered a control group. To balance patient characteristics (e.g. age, gender, and pre-A1c score), two-to-one propensity score matching method was used to identify two matched controls for each enrollee. Change in hemoglobin A1c from baseline to 3-6 months were compared among matched comparison groups. Results 13,582 patients were identified including 19 patients enrolled in diabetes education plus kitchen class, 640 patients in traditional diabetes education, and 12,923 patients referred but did not enroll. After matching, 1,318 matched patients were selected from the non-enrollees as the control group. The change in hemoglobin A1c was -0.49, -0.81, and -0.95 for the control group, diabetes education group, and diabetes education group with kitchen classes, respectively. Compared to the control group, both diabetes education groups had a greater reduction in hemoglobin A1c (difference of 0.32, 95% Confidence Interval [CI]=0.17, 0.48 for the diabetes education group; difference of 0.46, 95% CI=-0.28, 1.19) for the diabetes plus kitchen class group). Even though the diabetes education plus kitchen intervention had the largest reduction in hemoglobin A1c, the sample was small with large variation. Conclusions Integrating a teaching kitchen component into the traditional diabetes education curriculum is a promising approach that can further improve initial biometric outcomes. Future studies are warranted to demonstrate clinical effectiveness of this enhanced intervention. Financial Support Health Share Oregon Coordinated Care Organizationhttps://digitalcommons.psjhealth.org/milwaukie_family/1004/thumbnail.jp

Model-based engineering of widgets, user applications and servers compliant with ARINC 661 specification

International audienceThe purpose of ARINC 661 specification [1] is to define interfaces to a Cockpit Display System (CDS) used in any types of aircraft installations. ARINC 661 provides precise information for communication protocol between application (called User Applications) and user interface components (called widgets) as well as precise information about the widgets themselves. However, in ARINC 661, no information is given about the behaviour of these widgets and about the behaviour of an application made up of a set of such widgets. This paper presents the results of the application of a formal description technique to the various elements of ARINC 661 specification within an industrial project. This formal description technique called Interactive Cooperative Objects defines in a precise and non-ambiguous way all the elements of ARINC 661 specification. The application of the formal description techniques is shown on an interactive application called MPIA (Multi Purpose Interactive Application). Within this application, we present how ICO are used for describing interactive widgets, User Applications and User Interface servers (in charge of interaction techniques). The emphasis is put on the model-based management of the feel of the applications allowing rapid prototyping of the external presentation and the interaction techniques. Lastly, we present the CASE (Computer Aided Software Engineering) tool supporting the formal description technique and its new extensions in order to deal with large scale applications as the ones targeted at by ARINC 661 specification

Anchoring of proteins to lactic acid bacteria

The anchoring of proteins to the cell surface of lactic acid bacteria (LAB) using genetic techniques is an exciting and emerging research area that holds great promise for a wide variety of biotechnological applications. This paper reviews five different types of anchoring domains that have been explored for their efficiency in attaching hybrid proteins to the cell membrane or cell wall of LAB. The most exploited anchoring regions are those with the LPXTG box that bind the proteins in a covalent way to the cell wall. In recent years, two new modes of cell wall protein anchoring have been studied and these may provide new approaches in surface display. The important progress that is being made with cell surface display of chimaeric proteins in the areas of vaccine development and enzyme- or whole-cell immobilisation is highlighted.

Identification of sortase A (SrtA) substrates in Streptococcus uberis: evidence for an additional hexapeptide (LPXXXD) sorting motif

Sortase (a transamidase) has been shown to be responsible for the covalent attachment of proteins to the bacterial cell wall. Anchoring is effected on secreted proteins containing a specific cell wall motif toward their C-terminus; that for sortase A (SrtA) in Gram-positive bacteria often incorporates the sequence LPXTG. Such surface proteins are often characterized as virulence determinants and play important roles during the establishment and persistence of infection. Intramammary infection with Streptococcus uberis is a common cause of bovine mastitis, which impacts on animal health and welfare and the economics of milk production. Comparison of stringently produced cell wall fractions from S. uberis and an isogenic mutant strain lacking SrtA permitted identification of 9 proteins likely to be covalently anchored at the cell surface. Analysis of these sequences implied the presence of two anchoring motifs for S. uberis, the classical LPXTG motif and an additional LPXXXD motif

Fate of the H-NS–Repressed bgl Operon in Evolution of Escherichia coli

In the enterobacterial species Escherichia coli and Salmonella enterica, expression of horizontally acquired genes with a higher than average AT content is repressed by the nucleoid-associated protein H-NS. A classical example of an H-NS–repressed locus is the bgl (aryl-β,D-glucoside) operon of E. coli. This locus is “cryptic,” as no laboratory growth conditions are known to relieve repression of bgl by H-NS in E. coli K12. However, repression can be relieved by spontaneous mutations. Here, we investigated the phylogeny of the bgl operon. Typing of bgl in a representative collection of E. coli demonstrated that it evolved clonally and that it is present in strains of the phylogenetic groups A, B1, and B2, while it is presumably replaced by a cluster of ORFans in the phylogenetic group D. Interestingly, the bgl operon is mutated in 20% of the strains of phylogenetic groups A and B1, suggesting erosion of bgl in these groups. However, bgl is functional in almost all B2 isolates and, in approximately 50% of them, it is weakly expressed at laboratory growth conditions. Homologs of bgl genes exist in Klebsiella, Enterobacter, and Erwinia species and also in low GC-content Gram-positive bacteria, while absent in E. albertii and Salmonella sp. This suggests horizontal transfer of bgl genes to an ancestral Enterobacterium. Conservation and weak expression of bgl in isolates of phylogenetic group B2 may indicate a functional role of bgl in extraintestinal pathogenic E. coli

Sortase A Substrate Specificity in GBS Pilus 2a Cell Wall Anchoring

Streptococcus agalactiae, also referred to as Group B Streptococcus (GBS), is one of the most common causes of life-threatening bacterial infections in infants. In recent years cell surface pili have been identified in several Gram-positive bacteria, including GBS, as important virulence factors and promising vaccine candidates. In GBS, three structurally distinct types of pili have been discovered (pilus 1, 2a and 2b), whose structural subunits are assembled in high-molecular weight polymers by specific class C sortases. In addition, the highly conserved housekeeping sortase A (SrtA), whose main role is to link surface proteins to bacterial cell wall peptidoglycan by a transpeptidation reaction, is also involved in pili cell wall anchoring in many bacteria. Through in vivo mutagenesis, we demonstrate that the LPXTG sorting signal of the minor ancillary protein (AP2) is essential for pilus 2a anchoring. We successfully produced a highly purified recombinant SrtA (SrtAΔN40) able to specifically hydrolyze the sorting signal of pilus 2a minor ancillary protein (AP2-2a) and catalyze in vitro the transpeptidation reaction between peptidoglycan analogues and the LPXTG motif, using both synthetic fluorescent peptides and recombinant proteins. By contrast, SrtAΔN40 does not catalyze the transpeptidation reaction with substrate-peptides mimicking sorting signals of the other pilus 2a subunits (the backbone protein and the major ancillary protein). Thus, our results add further insight into the proposed model of GBS pilus 2a assembly, in which SrtA is required for pili cell wall covalent attachment, acting exclusively on the minor accessory pilin, representing the terminal subunit located at the base of the pilus

A Metalloproteinase Secreted by Streptococcus pneumoniae Removes Membrane Mucin MUC16 from the Epithelial Glycocalyx Barrier

The majority of bacterial infections occur across wet-surfaced mucosal epithelia, including those that cover the eye, respiratory tract, gastrointestinal tract and genitourinary tract. The apical surface of all these mucosal epithelia is covered by a heavily glycosylated glycocalyx, a major component of which are membrane-associated mucins (MAMs). MAMs form a barrier that serves as one of the first lines of defense against invading bacteria. While opportunistic bacteria rely on pre-existing defects or wounds to gain entry to epithelia, non opportunistic bacteria, especially the epidemic disease-causing ones, gain access to epithelial cells without evidence of predisposing injury. The molecular mechanisms employed by these non opportunistic pathogens to breach the MAM barrier remain unknown. To test the hypothesis that disease-causing non opportunistic bacteria gain access to the epithelium by removal of MAMs, corneal, conjunctival, and tracheobronchial epithelial cells, cultured to differentiate to express the MAMs, MUCs 1, 4, and 16, were exposed to a non encapsulated, non typeable strain of Streptococcus pneumoniae (SP168), which causes epidemic conjunctivitis. The ability of strain SP168 to induce MAM ectodomain release from epithelia was compared to that of other strains of S. pneumoniae, as well as the opportunistic pathogen Staphylococcus aureus. The experiments reported herein demonstrate that the epidemic disease-causing S. pneumoniae species secretes a metalloproteinase, ZmpC, which selectively induces ectodomain shedding of the MAM MUC16. Furthermore, ZmpC-induced removal of MUC16 from the epithelium leads to loss of the glycocalyx barrier function and enhanced internalization of the bacterium. These data suggest that removal of MAMs by bacterial enzymes may be an important virulence mechanism employed by disease-causing non opportunistic bacteria to gain access to epithelial cells to cause infection

IlsA, A Unique Surface Protein of Bacillus cereus Required for Iron Acquisition from Heme, Hemoglobin and Ferritin

The human opportunistic pathogen Bacillus cereus belongs to the B. cereus group that includes bacteria with a broad host spectrum. The ability of these bacteria to colonize diverse hosts is reliant on the presence of adaptation factors. Previously, an IVET strategy led to the identification of a novel B. cereus protein (IlsA, Iron-regulated leucine rich surface protein), which is specifically expressed in the insect host or under iron restrictive conditions in vitro. Here, we show that IlsA is localized on the surface of B. cereus and hence has the potential to interact with host proteins. We report that B. cereus uses hemoglobin, heme and ferritin, but not transferrin and lactoferrin. In addition, affinity tests revealed that IlsA interacts with both hemoglobin and ferritin. Furthermore, IlsA directly binds heme probably through the NEAT domain. Inactivation of ilsA drastically decreases the ability of B. cereus to grow in the presence of hemoglobin, heme and ferritin, indicating that IlsA is essential for iron acquisition from these iron sources. In addition, the ilsA mutant displays a reduction in growth and virulence in an insect model. Hence, our results indicate that IlsA is a key factor within a new iron acquisition system, playing an important role in the general virulence strategy adapted by B. cereus to colonize susceptible hosts