| Literature DB >> 31574230 |
Marzieh Rezaei1, Mohammad Rabbani Khorasgani1, Sayyed Hamid Zarkesh Esfahani1, Rahman Emamzadeh1, Hamid Abtahi2.
Abstract
The use of the food-grade bacterium Lactococcus lactis 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 L. lactis subsp. cremoris MG1363 by electrotransformation. Finally, the expression and purification of Omp16-IL2 fusion protein was investigated. This study reports the construction of a recombinant L. lactis expressing the Omp16-IL2 fusion protein as an oral Lactococcus-based vaccine, as compared with commonly used live attenuated vaccines, for future studies against brucellosis.Entities:
Keywords: Lactococcus lactis; Omp16-IL2 fusion protein; brucellose; brucellosis infection; clonage; cloning; protéine de fusion Omp16-IL2
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Year: 2019 PMID: 31574230 DOI: 10.1139/cjm-2019-0261
Source DB: PubMed Journal: Can J Microbiol ISSN: 0008-4166 Impact factor: 2.419