Expectations Regarding Gastein Healing Gallery Treatment and Their Connection to Health-Related Quality of Life.

The present study examines connections between patient expectations and health-related quality of life. We explore a key distinction between expectations about general health and expectations for functional improvement. Patients were 1444 individuals with multiple conditions experiencing chronic pain who were seeking treatment at the Gastein Healing Gallery in Böckstein, near Bad Gastein, Austria. In addition to measures of expectations, patients completed measures of pain, mental and physical health, life satisfaction, fatigue, and sleep problems. Structural equation models were used to fit a latent variable model where both expectation variables were used to predict health-related quality of life. Results showed that expectations regarding potential functional improvement resulting from treatments at the Gastein Healing Gallery were associated with improved health-related quality of life. Expectations about general health improvements related to treatment were not associated with health-related quality of life. To facilitate optimal healing, clinicians may decide to emphasize expectations about functional recovery when discussing treatment methods similar to those offered at the Gastein Healing Gallery, and in so doing, health-related quality of life may benefit.

Flagellin from Salmonella enteritidis Enhances the Immune Response of Fused F18 from Enterotoxigenic Escherichia coli.

F18 plays an important role in helping Enterotoxigenic Escherichia coli (ETEC) binds to specific receptors on small intestinal enterocytes, followed by secreting of toxins causing diarrhea in post-weaning piglets (post-weaning diarrhea, PWD). However, the F18 subunit vaccine is not sufficient to stimulate an immune response that can protect weaning pigs from F18-positive ETEC (F18+ETEC). Recently, a body of evidence shows that flagellin protein (FliC) helps to increase the immunity of fused proteins. Therefore, in this study, we combined FliC with F18 to enhance the immune response of F18. The f18 gene was obtained from F18+ETEC, then was fused with the fliC gene. The expression of recombinant FliC-F18 protein was induced by Isopropyl-beta-D-Thiogalactopyranoside (IPTG). The purified protein was tested in vivo in mouse models to evaluate the immunostimulation. Results showed that the fusion of FliC and F18 protein increased the production of anti-F18 antibodies. Besides, the anti-F18 antibody in the collected antiserum specifically identified F18+ETEC. This result provides proof-of-concept for the development of subunit vaccine to prevent PWD using F18 antigen.

Expression, Purification, and in vivo Evaluation of GFP-Fused M Cell Targeting Receptor Binding Domain of Protein FimH.

BACKGROUND: The number of oral vaccines is still limited due to many difficulties suffered in the intestinal environment, such as mucosal clearance, vast area, harsh conditions, deteriorative enzymes, impermeability, tolerance, etc. Numerous strategies have focused on directing antigen to the receptors of M cells, which is the main gateway to acquire and initiate specific responses to antigens in intestine. FimHrb is a receptor binding domain of type 1 of fimbriae from E. coli and Salmonella that can bind to GP2 receptor expressed exclusively on M cells. OBJECTIVE: In this study, we evaluated the potential of FimHrb for oral vaccine development via its ability to adhere M cells. METHODS: The coding gene of FimHrb fused Green Fluorescent Protein (GFP) was cloned and expressed intracellularly in E. coli host strain. The recombinant protein FimHrb-GFP was then purified by IMAC method through 6x His tag designed downstream of GFP. Finally, the purified protein was monitored its binding on murine M cells in Payer Patch region. RESULTS: Following the methods mentioned above, the coding gene FimHrb-GFP was successfully cloned into vector pET22b and intracellularly expressed in soluble form at low temperature induction. The purity and the recovered yield of this protein were 90% and 20%, respectively. After that, the adhesion of FimHrb-GFP was monitored in murine small intestine, which showed that the protein bound to Peyer Patch region and did not restrict on M cells. CONCLUSION: With the present data, we revealed a candidate protein FimHrb targeted receptor on M cells for oral vaccine development and other factors in E. coli would supplement FimH to provide the specific invasion of these bacteria via M cells.