Recent contributions in the field of the recombinant expression of disulfide bonded proteins in bacteria
نویسنده
چکیده
The production of heterologous disulfide bonded proteins in bacteria remains a biotechnological challenge. A rapid literature survey results in the identification of some interesting proposals, such as the option of producing functional proteins in the cytoplasm in the presence of sulfhydryl oxidases and isomerases. Furthermore, an ever-increasing number of applications refers to recombinant proteins displayed at the bacterial surface. Time will tell whether these developments will lead to universally accepted laboratory protocols.
منابع مشابه
Effect of Cysteamine on Cell Growth and IgG4 Production in Recombinant Sp2.0 Cells
The manipulation of redox potential in secretory pathway by thiol reducing agents can be a strategy to improve the production levels of disulfide-bonded proteins including recombinant antibodies. Here we have studied the influence of cysteamine on viability and the production level of IgG4 in Sp2.0 cells. For this purpose, the recombinant Sp2.0 cells producing an anti CD33 IgG4, were subjected ...
متن کاملEffect of Cysteamine on Cell Growth and IgG4 Production in Recombinant Sp2.0 Cells
The manipulation of redox potential in secretory pathway by thiol reducing agents can be a strategy to improve the production levels of disulfide-bonded proteins including recombinant antibodies. Here we have studied the influence of cysteamine on viability and the production level of IgG4 in Sp2.0 cells. For this purpose, the recombinant Sp2.0 cells producing an anti CD33 IgG4, were subjected ...
متن کاملSelecting appropriate hosts for recombinant proteins production: Review article
In recent years, the number of recombinant proteins used for therapeutic applications and industry has increased dramatically. Recombinant proteins are produced in many host organisms (microbial, insect, plant and mammalian cells). There are many factors to consider when choosing the optimal system for protein expression and purification including the mass, purity or solubility of the recombina...
متن کاملPlant-based expression systems for protein and antimicrobial peptide production
Molecular farming technology offers a unique advantage that almost any protein can be produced economically and safely under very controlled conditions. Besides traditional production systems, such as bacteria, yeasts, insects and mammal cell lines, plants can now be used to produce eukaryotic recombinant proteins, especially therapeutic ones. Their advantages as hosts for protein production in...
متن کاملA Novel Vector for Expression/Secretion of Properly Folded Eukaryotic Proteins: a Comparative Study on Cytoplasmic and Periplasmic Expression of Human Epidermal Growth Factor in E. coli
Expression of eukaryotic proteins in E. coli often results in their aggregation. Proper folding and solubility of therapeutical proteins are the pre-requisite for their bioactivity. This is not achieved in cytoplasmic expression in E. coli because of the absence of disulfide bonds formation. A novel expression/secretion vector was constructed which exploited β-lactamase signal sequence to trans...
متن کامل