Improving health from the inside
Autor: | Manuela Brandt, Christoph Pöhlmann, André Bleich, Florian Gunzer, Maike Hartmann, Sarah Förster, Mandy Thomas |
---|---|
Rok vydání: | 2013 |
Předmět: |
Signal peptide
Bioengineering Hemolysin General Medicine Biology Hemolysin Proteins medicine.disease_cause biology.organism_classification Applied Microbiology and Biotechnology OmpT Fusion protein Cell biology Microbiology medicine Cytokine secretion Escherichia coli Biotechnology Saccharomyces boulardii |
Zdroj: | Bioengineered. 4:172-179 |
ISSN: | 2165-5987 2165-5979 |
DOI: | 10.4161/bioe.22646 |
Popis: | The anti-inflammatory cytokine interleukin-10 and its viral homologs were chosen as model proteins for the development of drug delivery systems based on probiotic carriers like E. coli Nissle 1917, E. coli G3/10, and Saccharomyces boulardii. Exterior cytokine secretion was achieved by a modified E. coli hemolysin transporter. Release of interleukin-10 transported to the periplasm via the OmpF signal peptide was enabled by a T4 phage lysis system under control of the araC PBAD activator-promoter. The yield of interleukin-10 delivered by the phage lysis system was too low for functional analysis whereas the fusion protein secreted by the hemolysin transporter proved to be biologically inactive. Moreover, partial processing of the fusion protein by the E. coli membrane protease OmpT had no effect on the protein’s functionality. Using the α-mating factor signal sequence, the yeast S. boulardii proved to be suitable for secretory expression of biologically active viral interleukin-10. |
Databáze: | OpenAIRE |
Externí odkaz: |