Abstract:
: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.
journal_name
Bioengineeredjournal_title
Bioengineeredauthors
Pöhlmann C,Thomas M,Förster S,Brandt M,Hartmann M,Bleich A,Gunzer Fdoi
10.4161/bioe.22646subject
Has Abstractpub_date
2013-05-01 00:00:00pages
172-9issue
3eissn
2165-5979issn
2165-5987pii
22646journal_volume
4pub_type
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