The use of the food-grade bacterium as a new cell factory is a promising alternative expression system for producing a desired protein. The Omp16-IL2 fusion protein antigen was cloned, expressed, and purified in this study. The Omp16-IL2 fusion gene was designed and cloned in pGH plasmid with appropriate restriction sites and subcloned in pAMJ2008 expression vector digested with the same enzymes. The purified recombinant constructed pAMJ-rOmp-IL2 was introduced into subsp. MG1363 by electrotransformation. Finally, the expression and purification of Omp16-IL2 fusion protein was investigated. This study reports the construction of a recombinant expressing the Omp16-IL2 fusion protein as an oral -based vaccine, as compared with commonly used live attenuated vaccines, for future studies against brucellosis.
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http://dx.doi.org/10.1139/cjm-2019-0261 | DOI Listing |
Arch Microbiol
July 2021
Molecular and Medicine Research Center, Arak University of Medical Science, Arak, Islamic Republic of Iran.
This study was designed to introduce the recombinant Lactococcus lactis MG1363 as a cell factory candidate for production of recombinant Brucella melitensis Omp16-Human IL2 (r-Omp16-IL2) and to suggest it as a promising safe, non-pathogenic mucosal live vaccine against brucellosis. Three groups of BALB/c mice (10 mice per group) were intragastrically administrated with phosphate-buffered saline (PBS), L. lactis harboring the empty pAMJ2008 plasmid and with L.
View Article and Find Full Text PDFCan J Microbiol
January 2020
Molecular and Medicine Research Center, Arak University of Medical Science, Arak, Islamic Republic of Iran.
The use of the food-grade bacterium as a new cell factory is a promising alternative expression system for producing a desired protein. The Omp16-IL2 fusion protein antigen was cloned, expressed, and purified in this study. The Omp16-IL2 fusion gene was designed and cloned in pGH plasmid with appropriate restriction sites and subcloned in pAMJ2008 expression vector digested with the same enzymes.
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